B. Sykes

发表

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.

F. Richards, D. Wishart, B. Sykes, 1992, Biochemistry.

Neutrophil activation by monomeric interleukin-8.

B. Sykes, K. Rajarathnam, C. Kay, 1994, Science.

NMR solution structure of a highly stable de novo heterodimeric coiled‐coil

R. Hodges, B. Sykes, P. Mercier, 2004, Biopolymers.

Fluorotyrosine M13 coat protein: fluorine-19 nuclear magnetic resonance study of the motional properties of an integral membrane protein in phospholipid vesicles.

B. Sykes, J. Weiner, D. Hagen, 1978, Biochemistry.

Investigation of solvent accessibility of the fluorotyrosyl residues of M13 coat protein in deoxycholate micelles and phospholipid vesicles.

B. Sykes, J. Weiner, D. Hagen, 1979, Biochemistry.

19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles.

B. Sykes, J. Weiner, H. Dettman, 1982, Biophysical journal.

Structure‐based thermodynamic analysis of the dissociation of protein phosphatase‐1 catalytic subunit and microcystin‐LR docked complexes

Robert F. Boyko, B. Sykes, P. Lavigne, 2008, Protein science : a publication of the Protein Society.

The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data

D. Wishart, B. Sykes, 1994, Journal of biomolecular NMR.

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

R. Hodges, D. Wishart, B. Sykes, 1995, Journal of biomolecular NMR.

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure.

F. Richards, D. Wishart, B. Sykes, 1991, Journal of molecular biology.

Variation of metabolites in normal human urine

Erik J. Saude, B. Sykes, B. Rowe, 2007, Metabolomics.

Recommendations for the presentation of NMR structures of proteins and nucleic acids – IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy

K. Wüthrich, A. Bax, C. W. Hilbers, 1998, European journal of biochemistry.

Fourier transform ion cyclotron resonance mass spectrometric detection of small Ca2+-induced conformational changes in the regulatory domain of human cardiac troponin C

B. Sykes, M. Emmett, Weiqun Li, 1999, Journal of the American Society for Mass Spectrometry.

Interaction of cardiac troponin C with Ca(2+) sensitizer EMD 57033 and cardiac troponin I inhibitory peptide.

B. Sykes, L. Spyracopoulos, J. Putkey, 2000, Biochemistry.

Antifreeze proteins.

B. Sykes, P. Davies, Peter L. Davies, 1997, Current opinion in structural biology.

β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect

Michael J. Kuiper, Brian D. Sykes, Zongchao Jia, 2000, Nature.

Investigations of the effects of gender, diurnal variation, and age in human urinary metabolomic profiles.

Russ Greiner, Sirish L. Shah, James R. Wagner, 2007, Analytical chemistry.

Recommendations for the presentation of NMR structures of proteins and nucleic acids.

P E Wright, B D Sykes, K Wüthrich, 1998, Journal of molecular biology.

ORB, a homology-based program for the prediction of protein NMR chemical shifts

David S. Wishart, Wolfram Gronwald, Robert F. Boyko, 1997 .

Dipolar nuclear spin relaxation of 19F in multispin systems. Application to 19F labeled proteins

B. Sykes, W. Hull, 1975 .

NMR Approaches to the Characterization of the Interaction of Metal Ions with Proteins

B. Sykes, T. C. Williams, J. Shelling, 1986 .

Structural studies of calcium-binding proteins using nuclear magnetic resonance.

B. Sykes, D. Corson, L. Lee, 1985, Biophysical journal.

Proton nuclear magnetic resonance studies of the interaction of the lanthanide ions ytterbium and lutetium with apo- and calcium-saturated porcine intestinal calcium binding protein

B. Sykes, J. Shelling, T. Hofmann, 1985 .

Lanthanide-induced peptide folding: variations in lanthanide affinity and induced peptide conformation.

R. Hodges, B. Sykes, J. Gariépy, 1983, Biochemistry.

Proton nuclear magnetic resonance studies of porcine intestinal calcium binding protein.

B. Sykes, J. O'Neil, J. Shelling, 1983, Biochemistry.

Spectral studies on the calcium binding properties of bovine brain S-100b protein.

B. Sykes, C. Kay, R. Mani, 1983, Biochemistry.

Structure of the C-domain of Human Cardiac Troponin C in Complex with Ca2+ Sensitizer EMD 57033

B. Sykes, L. Spyracopoulos, R. Solaro, 2001 .

Structure of the Regulatory N-domain of Human Cardiac Troponin C in Complex with Human Cardiac Troponin I147–163 and Bepridil*

Brian D Sykes, B. Sykes, Xu Wang, 2002, The Journal of Biological Chemistry.

Ubiquinone-binding Site Mutations in the Saccharomyces cerevisiae Succinate Dehydrogenase Generate Superoxide and Lead to the Accumulation of Succinate*

B. Sykes, S. Szeto, S. Reinke, 2007, Journal of Biological Chemistry.

Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum.

B. Sykes, M. Schlesinger, H. Weingarten, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Measurement of 2H T1 and T1.rho. Relaxation Times in Uniformly 13C-Labeled and Fractionally 2H-Labeled Proteins in Solution

Brian D. Sykes, Toshio Yamazaki, Lewis E. Kay, 1995 .

Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein.

B. Sykes, J. Weiner, G. Henry, 1986, Biochemistry.

A 1H/19F minicoil NMR probe for solid-state NMR: application to 5-fluoroindoles.

B. Sykes, S. Graether, R. McDonald, 2006, Journal of magnetic resonance.

1H NMR derived metabolomic profile of neonatal asphyxia in umbilical cord serum: implications for hypoxic ischemic encephalopathy.

B. Sykes, G. Boylan, D. Broadhurst, 2013, Journal of proteome research.

Nuclear magnetic resonance determination of metal-protn distances in the EF site of carp parvalbumin using the susceptibility contribution to the line broadening of lanthanide-shifted resonances.

B. Sykes, L. Lee, 1980, Biochemistry.

Metabolomic biomarkers in a model of asthma exacerbation: urine nuclear magnetic resonance.

Erik J. Saude, B. Sykes, R. Somorjai, 2009, American journal of respiratory and critical care medicine.

The effect of haemolysis on the metabolomic profile of umbilical cord blood.

G B Boylan, B D Sykes, D. Wishart, 2015, Clinical biochemistry.

A nuclear magnetic resonance study of bovine pancreatic trypsin inhibitor. Tyrosine titrations and backbone NH groups.

B. Sykes, G. Snyder, S. Karplus, 1973, Biochemistry.

Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic .alpha.-helical peptides

R. Hodges, B. Sykes, N. Zhou, 1992 .

Disulfide bond mapping and structural characterization of spruce budworm antifreeze protein.

B. Sykes, C. Kay, P. Davies, 1998, European journal of biochemistry.

NMR STRUCTURAL STUDIES ON ANTIFREEZE PROTEINS

B. Sykes, P. Davies, F. Sönnichsen, 1998 .

Comparative modeling of the three‐dimensional structure of Type II antifreeze protein

B. Sykes, P. Davies, F. Sönnichsen, 1995, Protein science : a publication of the Protein Society.

Effect of internal rotation on nuclear magnetic relaxation times for macromolecules.

B. Sykes, A. Marshall, P. Schmidt, 1972, Biochemistry.

A novel Gerstmann-Sträussler-Scheinker disease mutation defines a precursor for amyloidogenic 8 kDa PrP fragments and reveals N-terminal structural changes shared by other GSS alleles

B. Sykes, G. Jansen, D. Westaway, 2018, PLoS pathogens.

Structural and Functional Analysis of Transmembrane XI of the NHE1 Isoform of the Na+/H+ Exchanger*

B. Sykes, L. Fliegel, Yongsheng Liu, 2009, Journal of Biological Chemistry.

Structure-function analysis of the adherence-binding domain on the pilin of Pseudomonas aeruginosa strains PAK and KB7.

R. Hodges, B. Sykes, C. McInnes, 1995, Biochemistry.

Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.

R. Hodges, B. Sykes, C. McInnes, 1996 .

Interaction of the receptor binding domains of Pseudomonas aeruginosa pili strains PAK, PAO, KB7 and P1 to a cross-reactive antibody and receptor analog: implications for synthetic vaccine design.

R. Hodges, B. Sykes, R. Irvin, 1997, Journal of molecular biology.

Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.

R. Hodges, B. Sykes, B. Tripet, 1997, Biochemistry.

Interaction of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK with a cross-reactive antibody: conformation of the bound peptide.

B. Sykes, R. Irvin, W. Wong, 2000, Biochemistry.

Letter to the Editor: Assignments of 1H and 15N resonances of the Pseudomonas aeruginosa K122-4 pilin monomer

B. Sykes, R. Irvin, M. Crump, 2001, Journal of biomolecular NMR.

Structure of a pilin monomer from Pseudomonas aeruginosa: implications for the assembly of pili.

B. Sykes, C. Slupsky, R. Irvin, 2001, The Journal of biological chemistry.

Proximity of two tryptophan residues in dihydrofolate reductase determined by 19F NMR

B. Sykes, J. Feeney, G. Roberts, 1978, Nature.

Isoform‐specific variation in the intrinsic disorder of troponin I

B. Sykes, Ryan M. B. Hoffman, 2008, Proteins.

Fluorine-19 nuclear magnetic resonance studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. A direct comparison of the effects of cis and trans cyclopropane ring and double-bond substituents on orientational order.

B. Sykes, R. McElhaney, P. Macdonald, 1985, Biochemistry.

Different interactions of Cro repressor dimer with the left and right halves of OR3 operator DNA.

B. Sykes, J. Baleja, W. Anderson, 1991, The Journal of biological chemistry.

Calcium-induced structural transition in the regulatory domain of human cardiac troponin C.

B D Sykes, B. Sykes, S. Sia, 1997, Biochemistry.

Interaction of cardiac troponin with cardiotonic drugs: a structural perspective.

I. M. Robertson, B. Sykes, Monica X. Li, 2008, Biochemical and biophysical research communications.

Structural based insights into the role of troponin in cardiac muscle pathophysiology

B. Sykes, Xu Wang, Monica X. Li, 2004, Journal of Muscle Research & Cell Motility.

Structure and Dynamics of the C-domain of Human Cardiac Troponin C in Complex with the Inhibitory Region of Human Cardiac Troponin I*

B. Sykes, D. Lindhout, 2003, Journal of Biological Chemistry.

Oncomodulin. 1H NMR and optical stopped-flow spectroscopic studies of its solution conformation and metal-binding properties.

B. Sykes, D. Corson, J. MacManus, 1987, The Journal of biological chemistry.

IUPAC-IUBMB-IUPAB INTER-UNION TASK GROUP ON THE STANDARDIZATION OF DATA BASES OF PROTEIN AND NUCLEIC ACID STRUCTURES DETERMINED BY NMR SPECTROSCOPY RECOMMENDATIONS FOR THE PRESENTATION OF NMR STRUCTURES OF PROTEINS AND NUCLEIC ACIDS

K. Wüthrich, A. Bax, P. Wright, 1998 .

Fluorine-19 nuclear magnetic resonance studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. Effects of methyl-branch substitution and of trans unsaturation upon membrane acyl-chain orientational order.

B. Sykes, R. McElhaney, P. Macdonald, 1983, Biochemistry.

Structural Characterization of Amyloidotic Antifreeze Protein Fibrils and Intermediates

B. Sykes, S. Graether, 2009, Journal of toxicology and environmental health. Part A.

Phosphorus-31 nuclear magnetic resonance studies of adenosine 5'-triphosphate bound to a nitrated derivative of G-actin.

B. Sykes, M. Brauer, 1981, Biochemistry.

1H MAS NMR of Donor Pancreatic Tissue is a Useful Predictor of Islet Viability Prior to Islet Isolation

B. Sykes, C. Slupsky, J. Lakey, 2020, bioRxiv.

Structure of type I antifreeze protein and mutants in supercooled water.

B. Sykes, C. Slupsky, S. Graether, 2001, Biophysical journal.

Binding of an Oligopeptide to a Specific Plane of Ice*

R. Hodges, B. Sykes, C. Kay, 1998, The Journal of Biological Chemistry.

Nitrotyrosine chelation of nuclear magnetic resonance shift probes in proteins: application to bovine pancreatic trypsin inhibitor.

B. Sykes, G. Snyder, T. Marinetti, 1977, Biochemistry.

Nuclear magnetic resonance determination of intramolecular distances in bovine pancreatic trypsin inhibitor using nitrotyrosine chelation of lanthanides.

B. Sykes, G. Snyder, T. Marinetti, 1976, Biochemistry.

The stepwise binding of small molecules to proteins. Nuclear magnetic resonance and temperature jump studies of the binding of 4-(N-acetylaminoglucosyl)-N-acetylglucosamine to lysozyme.

B. Sykes, S. Halford, S. Patt, 1975, Biochemistry.

Internal pH indicators for biomolecular NMR

B. Sykes, T. C. Williams, O. Baryshnikova, 2008, Journal of biomolecular NMR.

Side-chain dynamics of a detergent-solubilized membrane protein: measurement of tryptophan and glutamine hydrogen-exchange rates in M13 coat protein by 1H NMR spectroscopy.

B. Sykes, J. O'Neil, 1989, Biochemistry.

Rewiring AMPK and mitochondrial retrograde signaling for metabolic control of aging and histone acetylation in respiratory-defective cells.

B. Sykes, M. C. Schultz, T. Huan, 2014, Cell reports.

Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy

B. Sykes, M. Daley, 2004, Journal of biomolecular NMR.

Backbone dynamics of receptor binding and antigenic regions of a Pseudomonas aeruginosa pilin monomer.

B. Sykes, L. Spyracopoulos, R. Irvin, 2001, Biochemistry.

NMR Studies of Protein Sidechain Dynamics

W. Gronwald, L. Kay, B. Sykes, 1998 .

31P-NMR study of the phospholipid moiety of lipophorin subspecies.

B. Sykes, R. Ryan, H. Liu, 1992, Biochemistry.

Optimizing fluorine labelling for 19F solid-state NMR in oriented biological systems

Brittney A. Klein, I. M. Robertson, B. Sykes, 2020, Journal of Biomolecular NMR.

Editorial

B. Sykes, 2011, Journal of biomolecular NMR.

The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions.

B. Sykes, V. Booth, D. Keizer, 2002, Biochemistry.

Nascent β Structure in the Elongated Hydrophobic Region of a Gerstmann-Sträussler-Scheinker PrP Allele.

B. Sykes, D. Westaway, Ze-Lin Fu, 2019, Journal of molecular biology.

Enhancing the activity of a beta-helical antifreeze protein by the engineered addition of coils.

B. Sykes, P. Davies, C. Marshall, 2004, Biochemistry.

Folding and structural characterization of highly disulfide-bonded beetle antifreeze protein produced in bacteria.

B. Sykes, C. Kay, Y. Liou, 2000, Protein expression and purification.

A diminished role for hydrogen bonds in antifreeze protein binding to ice.

R. Hodges, B. Sykes, C. Kay, 1997, Biochemistry.

Structural Characterization of a Low Density Lipoprotein Receptor-active Apolipoprotein E Peptide, ApoE3-(126–183)*

B. Sykes, C. Kay, V. Raussens, 2000, The Journal of Biological Chemistry.

NMR evidence for a conformational adaptation of apolipophorin III upon lipid association

B. Sykes, R. Ryan, Jianjun Wang, 1998 .

Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins

B. Sykes, V. Narayanaswami, R. Ryan, 1998, Protein science : a publication of the Protein Society.

Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C.

B. Sykes, L. Spyracopoulos, M. X. Li, 1999, Biochemistry.

A Common Phenotype Polymorphism in Mammalian Brains Defined by Concomitant Production of Prolactin and Growth Hormone

Inyoul Y. Lee, L. Hood, B. Sykes, 2016, PloS one.

Backbone dynamics of a model membrane protein: measurement of individual amide hydrogen-exchange rates in detergent-solubilized M13 coat protein using 13C NMR hydrogen/deuterium isotope shifts.

B. Sykes, J. Weiner, G. Henry, 1987, Biochemistry.

NMR analysis of neutrophil activation in sputum samples from patients with cystic fibrosis

Erik J. Saude, B. Sykes, Paige Lacy, 2004, Magnetic resonance in medicine.

31P and 35Cl nuclear magnetic resonance measurements of anion transport in human erythrocytes.

B. Sykes, R. Reithmeier, M. Brauer, 1985, The Journal of biological chemistry.

Freezing of a fish antifreeze protein results in amyloid fibril formation.

B. Sykes, C. Slupsky, S. Graether, 2003, Biophysical journal.

Conformation of retinal isomers.

M. Karplus, B. Sykes, R. Rowan, 1974, Biochemistry.

Observation of multiple myosin subfragment 1-ADP-fluoroberyllate complexes by 19F NMR spectroscopy.

B. Sykes, M. Ikebe, G. Henry, 1993, Biochemistry.

Disposition and dynamics: interdomain orientations in troponin.

B. Sykes, Ryan M. B. Hoffman, 2007, Advances in experimental medicine and biology.

Stoichiometry of calcium binding to a synthetic heterodimeric troponin‐C domain

R. Hodges, B. Sykes, G. Shaw, 1992, Biopolymers.

Design of a model Ca2+-binding protein with a single Ca2+-binding site and enhanced metal ion affinity

R. Hodges, B. Sykes, C. Kay, 1991 .

Phosphorus-31 nuclear magnetic resonance studies of the adenosine 5'-triphosphate-calcium-G-actin complex.

B. Sykes, M. Brauer, 1981, Biochemistry.

Experimental evidence for the role of cross-relaxation in proton nuclear magnetic resonance spin lattice relaxation time measurements in proteins.

B. Sykes, W. Hull, G. Snyder, 1978, Biophysical journal.

A method for the facile solid-phase synthesis of gramicidin S and its analogs

R. Hodges, D. Wishart, B. Sykes, 1996, Letters in Peptide Science.

Structure‐function relationship in the globular type III antifreeze protein: Identification of a cluster of surface residues required for binding to ice

B. Sykes, P. Davies, F. Sönnichsen, 1994, Protein science : a publication of the Protein Society.

Structure effects of double D-amino acid replacements: a nuclear magnetic resonance and circular dichroism study using amphipathic model helices.

R. Hodges, B. Sykes, G. Krause, 1995, Biochemistry.

Toward protein structure in situ: comparison of two bifunctional rhodamine adducts of troponin C.

B. Sykes, Yin-Biao Sun, M. Irving, 2007, Biophysical journal.

Characterization of sodium transport in Acholeplasma laidlawii B cells and in lipid vesicles containing purified A. laidlawii (Na+-Mg2+)-ATPase by using nuclear magnetic resonance spectroscopy and 22Na tracer techniques

B. Sykes, R. Lewis, R. McElhaney, 1988, Journal of bacteriology.

Phenylalanyl and tyrosyl side chain mobility in the M13 coat protein reconstituted in phospholipid vesicles

B. Sykes, J. Weiner, H. Dettman, 1984 .

Adam's Curse: A Future without Men

B. Sykes, 2003 .

Blood of the Isles: Exploring the Genetic Roots of Our Tribal History

B. Sykes, 2006 .

In situ orientations of protein domains: troponin C in skeletal muscle fibers.

B. Sykes, P. Mercier, Yin-Biao Sun, 2003, Molecular cell.

Approaches to Protein-Ligand Structure Determination by NMR Spectroscopy: Applications in Drug Binding to the Cardiac Regulatory Protein Troponin C

I. M. Robertson, B. Sykes, Sandra E. Pineda-Sanabria, 2012 .

Solution structure of the regulatory domain of human cardiac troponin C in complex with the switch region of cardiac troponin I and W7: the basis of W7 as an inhibitor of cardiac muscle contraction.

I. M. Robertson, B. Sykes, M. Oleszczuk, 2010, Journal of molecular and cellular cardiology.

Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1

B. Sykes, K. Rajarathnam, M. Baggiolini, 1997, The EMBO journal.

1H NMR studies of interleukin 8 analogs: characterization of the domains essential for function.

B. Sykes, K. Rajarathnam, I. Clark‐Lewis, 1994, Biochemistry.

Analysis of cooperativity observed in pH titrations of proton nuclear magnetic resonances of histidine residues of rabbit cardiac tropomyosin.

B. Sykes, B. Edwards, 1981, Biochemistry.

Nuclear magnetic resonance evidence for the coexistence of several conformational states of rabbit cardiac and skeletal tropomyosins.

B. Sykes, B. Edwards, 1980, Biochemistry.

Strategies for the uses of lanthanide NMR shift probes in the determination of protein structure in solutio. Application to the EF calcium binding site of carp parvalbumin.

B. Sykes, L. Lee, 1980, Biophysical journal.

The temperature dependence of lanthanide-induced 1H NMR shifts observed for the interaction of Yb3+ with the calcium-binding protein parvalbumin

B. Sykes, Lana Lee, 1980 .

13C and 113Cd NMR studies of the chelation of metal ions by the calcium binding protein parvalbumin.

B. Sykes, D. Corson, M. E. Bjornson, 1985, Journal of inorganic biochemistry.

Foundations and Future of Molecular Pharmacology

B. Sykes, P. Taylor, P. Sigler, 1995 .

1H, 13C and 15N chemical shift referencing in biomolecular NMR

Eric Oldfield, D. Wishart, H. Dyson, 1995, Journal of biomolecular NMR.

Feasibility of trifluoromethyl TROSY NMR at high magnetic fields

Brittney A. Klein, B. Sykes, 2019, Journal of Biomolecular NMR.

Concanavalin A: a stopped flow nuclear magnetic resonance study of conformational changes induced by Mn++, Ca++, and alpha-methyl-D-mannoside.

B. Sykes, J. J. Grimaldi, 1975, The Journal of biological chemistry.

Stopped-flow nuclear magnetic resonance spectroscopy

B. Sykes, C. McMurray, J. J. Grimaldi, 1972 .

University of Alberta “OMICs” Conference, June 17, 2013: Conference Program and Abstracts

Fang Wu, David S. Wishart, Sambasivarao Damaraju, 2013 .

INTERNAL MOBILITY IN THE STRUCTURE OF TROPOMYOSIN AND IN THE TROPONIN—TROPOMYOSIN COMPLEX

B. Sykes, B. Edwards, Lana Lee, 1978 .

STOPPED FLOW FOURIER TRANSFORM NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, AN APPLICATION TO THE ALPHA-CHYMOTRYPSIN-CATALYZED HYDROLYSIS OF TERT.-BUTYL-L-PHENYLALANINE

B. Sykes, J. J. Grimaldi, 1975 .

In Vitro and in Situ Structure and Function of the Cardiac Troponin C Familial Hypertrophic Cardiomyopathy-Linked Mutation, L29Q

I. M. Robertson, B. Sykes, Yin-Biao Sun, 2014 .

Structural and functional consequences of the cardiac troponin C L48Q Ca(2+)-sensitizing mutation.

I. M. Robertson, V. Daggett, B. Sykes, 2012, Biochemistry.

Effect of temperature and the F27W mutation on the Ca2+ activated structural transition of trout cardiac troponin C.

B. Sykes, G. Tibbits, T. Gillis, 2003, Biochemistry.

Energetics of the induced structural change in a Ca2+ regulatory protein: Ca2+ and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C.

B. Sykes, R. McKay, M. X. Li, 2000, Biochemistry.

Bacterial overexpression, isotope enrichment, and NMR analysis of the N-terminal domain of human apolipoprotein E.

G. Francis, B. Sykes, C. Kay, 1997, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Pulling the calcium trigger

B. Sykes, 2003, Nature Structural Biology.

The NMR Structure of a Bifunctional Rhodamine Labeled N-domain of Troponin C inComplex with the Regulatory 'Switch' Peptide from Troponin I

B. Sykes, P. Mercier, M. Irving, 2003 .

NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.

B. Sykes, P. Mercier, M. Irving, 2003, Biochemistry.

Shooting blanks: Ca2+-free signaling.

B. Sykes, 2007, Structure.

Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding.

B. Sykes, W. Hull, 1976, Biochemistry.

Fluorotyrosine alkaline phosphatase. 19F nuclear magnetic resonance relaxation times and molecular motion of the individual fluorotyrosines.

B. Sykes, W. Hull, 1974, Biochemistry.

1H NMR spectroscopic studies of calcium-binding proteins. 3. Solution conformations of rat apo-alpha-parvalbumin and metal-bound rat alpha-parvalbumin.

B. Sykes, C. Kay, D. Corson, 1986, Biochemistry.

Structural and functional consequences of the cardiac troponin C L48Q Ca(2+)-sensitizing mutation.

Dan Wang, Valerie Daggett, Brian D. Sykes, 2012, Biochemistry.

The binding of W7, an inhibitor of striated muscle contraction, to cardiac troponin C.

B. Sykes, Ryan M. B. Hoffman, Monica X. Li, 2005, Biochemistry.

Structure determination by NMR. Isotope labeling.

B. Sykes, D. Corson, Monica X. Li, 2002, Methods in molecular biology.

An improved synthesis of α-13C glycine and heteronuclear NMR studies of its incorporation into thioredoxin

F. Richards, D. Wishart, B. Sykes, 1992 .

Complete tyrosine assignments in the high-field 1H nuclear magnetic resonance spectrum of bovine pancreatic trypsin inhibitor selectively reduced and carboxamidomethylated at cystine 14-38.

B. Sykes, G. Snyder, R. Rowan, 1976, Biochemistry.

Complete tyrosine assignments in the high field 1H nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitor.

B. Sykes, G. Snyder, R. Rowan, 1975, Biochemistry.

Development of the Structural Basis for Antimicrobial and Hemolytic Activities of Peptides Based on Gramicidin S and Design of Novel Analogs Using NMR Spectroscopy*

B D Sykes, R. Hodges, B. Sykes, 2000, The Journal of Biological Chemistry.

Alternative roles for putative ice-binding residues in type I antifreeze protein.

R. Hodges, B. Sykes, C. Kay, 1999, Biochemistry.

The seven daughters of Eve

Brian D. Sykes, B. Sykes, 2001 .

Optimizing oriented planar-supported lipid samples for solid-state protein NMR.

B. Sykes, J. Rainey, 2005, Biophysical journal.

Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli

B. Sykes, P. Hwang, Jonathan S Pan, 2014, FEBS letters.

The calcium sensitizer drug MCI-154 binds the structural C-terminal domain of cardiac troponin C

B. Sykes, F. West, M. J. Lemieux, 2018, Biochemistry and biophysics reports.

A structural and functional perspective into the mechanism of Ca2+-sensitizers that target the cardiac troponin complex.

I. M. Robertson, B. Sykes, Yin-Biao Sun, 2010, Journal of molecular and cellular cardiology.

Defining the Binding Site of Levosimendan and Its Analogues in a Regulatory Cardiac Troponin C−Troponin I Complex

I. M. Robertson, B. Sykes, Monica X. Li, 2008, Biochemistry.

Distances obtained from nuclear magnetic resonance nuclear Overhauser effect and relaxation time. Measurements in organic structure determination. Distances involving internally rotating methyl groups. Application to cis- and trans-crotonaldehyde

J. Mccammon, B. Sykes, R. Rowan, 1974 .

Dissociation of Antimicrobial and Hemolytic Activities in Cyclic Peptide Diastereomers by Systematic Alterations in Amphipathicity*

B D Sykes, R. Hodges, B. Sykes, 1999, The Journal of Biological Chemistry.

Improved synthetic methods for the selective deuteration of aromatic amino acids: applications of selective protonation towards the identification of protein folding intermediates through nuclear magnetic resonance.

F. Richards, D. Wishart, B. Sykes, 1993, Biochimica et biophysica acta.

Biomolecular structure and function

B. Sykes, P. Agris, R. Loeppky, 1978 .

Solvent-induced deuterium isotope effects on 19F chemical shifts of some substituted fluorobenzenes. Formation of inclusion complexes

B. Sykes, P. Hansen, H. Dettman, 1985 .

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.

R. Hodges, B. Sykes, J. V. Van Eyk, 1992, Biochemistry.

Calcium-induced dimerization of troponin C: mode of interaction and use of trifluoroethanol as a denaturant of quaternary structure.

B. Sykes, C. Kay, C. Slupsky, 1995, Biochemistry.

Lactam bridge stabilization of alpha-helices: the role of hydrophobicity in controlling dimeric versus monomeric alpha-helices.

R. Hodges, B. Sykes, C. Kay, 1996, Biochemistry.

Nuclear magnetic resonance studies of the dynamic aspects of molecular structure and interaction in biological systems.

B D Sykes, M D Scott, B. Sykes, 1972, Annual review of biophysics and bioengineering.

HMDB: the Human Metabolome Database

Ying Zhang, David S. Wishart, Dean Cheng, 2007, Nucleic Acids Res..

Fluorine-19 nuclear magnetic resonance studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. Gel-state disorder in the presence of methyl iso- and anteiso-branched-chain substituents.

B. Sykes, R. McElhaney, P. Macdonald, 1985, Biochemistry.

Fluorotyrosine alkaline phosphatase: internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in proteins.

B. Sykes, W. Hull, 1975, Journal of molecular biology.

Role of interchain α‐helical hydrophobic interactions in Ca2+ affinity, formation, and stability of a two‐site domain in troponin C

R. Hodges, B. Sykes, C. Kay, 1992, Protein science : a publication of the Protein Society.

Metal ion binding by proteins: Current Opinion in Structural Biology 1992, 2:57…-60

Brian D. Sykes, B. Sykes, G. Shaw, 1992 .

Metal Ion Induced Folding of a de Novo Designed Coiled-Coil Peptide

R. Hodges, B. Sykes, C. Kay, 1998 .

Interaction of tropomyosin and troponin T: a proton nuclear magnetic resonance study.

J. Brisson, B. Sykes, L. Smillie, 1986, Biochemistry.

Contact and dipolar contributions to lanthanide-induced NMR shifts of amino acid and peptide models for calcium binding sites in proteins

R. Hodges, B. Sykes, J. Shelling, 1984 .

The ice-binding site of sea raven antifreeze protein is distinct from the carbohydrate-binding site of the homologous C-type lectin.

W. Gronwald, B. Sykes, P. Davies, 1998, Biochemistry.

The solution structure of type II antifreeze protein reveals a new member of the lectin family.

W. Gronwald, B. Sykes, P. Davies, 1998, Biochemistry.

Use of lanthanide-induced nuclear magnetic resonance shifts for determination of protein structure in solution: EF calcium binding site of carp parvalbumin.

B. Sykes, L. Lee, 1983, Biochemistry.

Laser photochemically induced dynamic nuclear polarization proton nuclear magnetic resonance studies on three homologous calcium binding proteins: cardiac troponin-C, skeletal troponin-C, and calmodulin.

B. Sykes, C. Kay, M. Hincke, 1981, Biochemistry.

Hydrogen-1 nuclear magnetic resonance investigation on bovine cardiac troponin C. Comparison of tyrosyl assignments and calcium-induced structural changes to those of two homologous proteins, rabbit skeletal troponin C and bovine brain calmodulin.

B. Sykes, C. Kay, M. Hincke, 1981, Biochemistry.

Proton nuclear magnetic resonance determination of the sequential ytterbium replacement of calcium in carp parvalbumin.

B. Sykes, L. Lee, 1981, Biochemistry.

Lanthanide interactions with nitrotyrosine. A specific binding site for nuclear magnetic resonance shift probes in proteins.

B. Sykes, G. Snyder, T. Marinetti, 1975, Journal of the American Chemical Society.

An application of transient nuclear magnetic resonance methods to the measurement of biological exchange rates. The interaction of trifluoroacetyl-D-phenylalanine with the chymotrypsins.

B. Sykes, 1969, Journal of the American Chemical Society.

A nuclear magnetic resonance study of the inhibition of lysozyme by N-acetyl-D-glucosamine and di-N-acetyl-D-glucosamine.

B. Sykes, C. Parravano, 1969, The Journal of biological chemistry.

Urine stability for metabolomic studies: effects of preparation and storage

Brian D. Sykes, Erik J. Saude, B. Sykes, 2007, Metabolomics.

The nonhelical structure of antifreeze protein type III.

B D Sykes, B. Sykes, P. Davies, 1993, Science.

Backbone dynamics of the human cc chemokine eotaxin: Fast motions, slow motions, and implications for receptor binding

B. Sykes, L. Spyracopoulos, Key‐Sun Kim, 1999, Protein science : a publication of the Protein Society.

Solution Structure of Eotaxin, a Chemokine That Selectively Recruits Eosinophils in Allergic Inflammation*

B. Sykes, K. Rajarathnam, Key‐Sun Kim, 1998, The Journal of Biological Chemistry.

RECENT ADVANCES IN METHODOLOGY: NUCLEAR MAGNETIC RESONANCE *

B. Sykes, W. Hull, 1973 .

Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein‐3

B. Sykes, K. Rajarathnam, Key‐Sun Kim, 1996, FEBS letters.

Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein

B. Sykes, P. Davies, F. Sönnichsen, 1993, Protein science : a publication of the Protein Society.

1H NMR spectroscopic studies of calcium-binding proteins. 1. Stepwise proteolysis of the C-terminal alpha-helix of a helix-loop-helix metal-binding domain.

L. Kay, B. Sykes, D. Corson, 1986, Biochemistry.

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

B D Sykes, R. Hodges, D. Wishart, 1995, Journal of biomolecular NMR.

A transient nuclear magnetic resonance study of the kinetics of methyl N-acetyl-D-glucosaminide inhibition of lysozyme.

B. Sykes, 1969, Biochemistry.

Laser photo-CIDNP 1H NMR studies of lysozyme, ovalbumin, and their interactions☆

H. Vogel, B. Sykes, 1984 .

Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction.

B. Sykes, P. Davies, F. Sönnichsen, 1996, Structure.

Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice.

B. Sykes, P. Davies, F. Sönnichsen, 1996, Biophysical journal.

Characterization of γ-Radiation Induced Decomposition Products of Thymidine-Containing Dinucleoside Monophosphates by Nuclear Magnetic Resonance Spectroscopy

B. Sykes, J. Baleja, G. W. Buchko, 1993 .

Ring orientation in -ionone and retinals.

M. Karplus, B. Honig, B. Sykes, 1971, Proceedings of the National Academy of Sciences of the United States of America.

A carbon-13 nuclear magnetic resonance study of the visual chromophores and model compounds.

B. Sykes, R. Rowan, 1974, Journal of the American Chemical Society.

A 1-H nuclear magnetic resonance determination of the conformations of the polyene chain portions of 9-cis- and 13-cis-retinal in solution.

B. Sykes, R. Rowan, 1975, Journal of the American Chemical Society.

31P nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH.

B. Sykes, S. Halford, W. Hull, 1976, Biochemistry.

Characterization of a novel weak interaction between MUC1 and Src-SH3 using nuclear magnetic resonance spectroscopy.

B. Sykes, J. Hugh, Nirosha Gunasekara, 2012, Biochemical and biophysical research communications.

Chemical shifts as a tool for structure determination.

B D Sykes, D. Wishart, B. Sykes, 1994, Methods in enzymology.

A (1)H NUCLEAR MAGNETIC RESONANCE DETERMINATION OF THE CONFORMATIONS OF THE POLYENE CHAIN PORTIONS OF 9‐CIS‐ AND 13‐CIS‐RETINAL IN SOLUTION

B. Sykes, R. Rowan, 1975 .

Recommendations for the presentation of NMR structures of proteins and nucleic acids (IUPAC Recommendations 1998)

K. Wüthrich, A. Bax, C. W. Hilbers, 1998 .

Solution structure of a DNA duplex containing the potent anti-poxvirus agent cidofovir.

Wendy C. Magee, B. Sykes, S. Chatterjee, 2011, Journal of the American Chemical Society.

Phosphorus-31 nuclear magnetic resonance studies of phosphorylated proteins.

B. Sykes, M. Brauer, 1984, Methods in enzymology.

Thermotropic phase behavior of model membranes composed of phosphatidylcholines containing cis-monounsaturated acyl chain homologues of oleic acid: differential scanning calorimetric and 31P NMR spectroscopic studies.

B D Sykes, B. Sykes, R. Lewis, 1988, Biochemistry.

[13] Fluorine nuclear magnetic resonance studies of proteins

B. Sykes, W. Hull, 1978 .

Determination of the 19F NMR chemical shielding tensor and crystal structure of 5-fluoro-dl-tryptophan.

B. Sykes, R. McDonald, Jeffrey S Devries, 2007, Journal of magnetic resonance.

Solution conformation of purine-pyrimidine DNA octamers using nuclear magnetic resonance, restrained molecular dynamics and NOE-based refinement.

B. Sykes, J. Van De Sande, J. Baleja, 1990, Journal of molecular biology.

Targeting the sarcomere to correct muscle function

Brian D. Sykes, B. Sykes, P. Hwang, 2015, Nature Reviews Drug Discovery.

Water Eliminated Fourier Transform NMR Spectroscopy

B. Sykes, S. Patt, 1972 .

Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase.

B. Sykes, S. P. Williams, W. A. Bridger, 1985, Biochemistry.

Mapping the Interacting Regions between Troponins T and C

R. Hodges, B. Sykes, B. Tripet, 2001, The Journal of Biological Chemistry.

Nuclear magnetic resonance studies of a Ca2+-binding fragment of troponin C.

E. R. Birnbaum, B. Sykes, 1978, Biochemistry.

An interplay between protein disorder and structure confers the Ca2+ regulation of striated muscle.

B. Sykes, Ryan M. B. Hoffman, T. Blumenschein, 2006, Journal of molecular biology.

High‐yield expression of isotopically labeled peptides for use in NMR studies

B. Sykes, D. Lindhout, D. Schieve, 2003, Protein science : a publication of the Protein Society.

The structural and functional effects of the familial hypertrophic cardiomyopathy-linked cardiac troponin C mutation, L29Q

I. M. Robertson, B. Sykes, Yin-Biao Sun, 2015, Journal of molecular and cellular cardiology.

Structure of Cardiac Muscle Troponin C Unexpectedly Reveals a Closed Regulatory Domain*

B. Sykes, S. Sia, L. Spyracopoulos, 1997, The Journal of Biological Chemistry.

A 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I

B. Sykes, C. Slupsky, G. Shaw, 1992, Protein science : a publication of the Protein Society.

Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: influence of PKA phosphorylation and involvement in cardiomyopathies.

B. Sykes, Monica X. Li, O. Baryshnikova, 2008, Journal of molecular biology.

Purification and characterization of troponin C from pike muscle: a comparative spectroscopic study with rabbit skeletal muscle troponin C.

B. Sykes, C. Kay, K. Oikawa, 1982, Biochemistry.

Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

B. Sykes, C. Slupsky, L. Smillie, 1995, Protein science : a publication of the Protein Society.

Interaction of the Second Binding Region of Troponin I with the Regulatory Domain of Skeletal Muscle Troponin C as Determined by NMR Spectroscopy*

R. Hodges, B. Sykes, R. McKay, 1997, The Journal of Biological Chemistry.

Interaction of troponin I and troponin C: use of the two-dimensional transferred nuclear Overhauser effect to determine the structure of a Gly-110 inhibitory troponin I peptide analog when bound to cardiac troponin C.

R. Hodges, B. Sykes, J. V. Van Eyk, 1992, Biochimica et biophysica acta.

Calcium-dependent inhibitory region of troponin: a proton nuclear magnetic resonance study on the interaction between troponin C and the synthetic peptide N alpha-acetyl[FPhe106]TnI-(104-115) amide.

R. Hodges, B. Sykes, P. Cachia, 1983, Biochemistry.

Quantification of the calcium‐induced secondary structural changes in the regulatory domain of troponin‐C

B. Sykes, S. Tsuda, S. Gagné, 1994, Protein science : a publication of the Protein Society.

X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme

D. Phillips, B. Sykes, M. James, 1979, Nature.

The HoxB1 hexapeptide is a prefolded domain: Implications for the Pbx1/Hox interaction

B. Sykes, C. Slupsky, D. Sykes, 2001, Protein science : a publication of the Protein Society.

The NMR angle on troponin C.

Brian D. Sykes, Ryan T. McKay, B. Sykes, 1998, Biochemistry and cell biology = Biochimie et biologie cellulaire.

The cryoprotective effects of dimethyl sulfoxide on human bone marrow as studied by 31P nuclear magnetic resonance spectroscopy

B. Sykes, M. Brauer, A. Janowska-Wieczorek, 1986, Magnetic resonance in medicine.

Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.

R. Hodges, B. Sykes, C. Kay, 1998, Journal of molecular biology.

Unusual beta-sheet periodicity in small cyclic peptides.

W. Gronwald, R. Hodges, D. Wishart, 1998, Nature structural biology.

Expression of Saccharomyces cerevisiae Sdh3p and Sdh4p Paralogs Results in Catalytically Active Succinate Dehydrogenase Isoenzymes*

B. Sykes, S. Reinke, B. Lemire, 2012, The Journal of Biological Chemistry.

The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C

B. Sykes, P. Hwang, D. Corson, 2014, Proceedings of the National Academy of Sciences.

Formation of the stable myosin-ADP-aluminum fluoride and myosin-ADP-beryllium fluoride complexes and their analysis using 19F NMR.

B. Sykes, M. Ikebe, S. Maruta, 1993, The Journal of biological chemistry.

Interaction of troponin I and troponin C. Use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory troponin I peptide when bound to skeletal troponin C.

B. Sykes, A. Campbell, 1991, Journal of molecular biology.

Proton nuclear magnetic resonance investigation of synthetic calcium-binding peptides.

R. Hodges, B. Sykes, J. Gariépy, 1982, Biochemistry.

Reversible Covalent Binding to Cardiac Troponin C by the Ca2+-Sensitizer Levosimendan.

I. M. Robertson, B. Sykes, Yin-Biao Sun, 2016, Biochemistry.

Elucidation of Isoform-dependent pH Sensitivity of Troponin I by NMR Spectroscopy*

I. M. Robertson, B. Sykes, Monica X. Li, 2011, The Journal of Biological Chemistry.

Conformation of the critical pH sensitive region of troponin depends upon a single residue in troponin I.

I. M. Robertson, B. Sykes, Peter C. Holmes, 2014, Archives of biochemistry and biophysics.

Relative stabilities of synthetic peptide homo‐ and heterodimeric troponin‐C domains

R. Hodges, B. Sykes, C. Kay, 1994, Protein science : a publication of the Protein Society.

1H-NMR resonance assignments, secondary structure, and global fold of the TR1C fragment of turkey skeletal troponin C in the calcium-free state.

B. Sykes, W. Findlay, 1993, Biochemistry.

Spectroscopic analysis of a methionine-48 to tyrosine mutant of chicken troponin C.

B. Sykes, C. Kay, L. Smillie, 1992, Biochemistry.

Conformation of a troponin-I peptide bound to troponin-C as determined by 1H NMR.

B. Sykes, A. Campbell, 1989, Advances in experimental medicine and biology.

Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2*

B. Sykes, Asad Ullah, L. Fliegel, 2013, The Journal of Biological Chemistry.

Structural and Functional Analysis of Transmembrane Segment VI of the NHE1 Isoform of the Na+/H+ Exchanger*

B. Sykes, L. Fliegel, Brian L. Lee, 2010, The Journal of Biological Chemistry.

Structural and functional insights into the cardiac Na⁺/H⁺ exchanger.

B. Sykes, L. Fliegel, Brian L. Lee, 2013, Journal of molecular and cellular cardiology.

The Role of Side Chain Conformational Flexibility in Surface Recognition by Tenebrio Molitor Antifreeze Protein

B. Sykes, M. Daley, Brian D. Sykes, 2003 .

Structural and functional analysis of extracellular loop 4 of the Nhe1 isoform of the Na(+)/H(+) exchanger.

B. Sykes, L. Fliegel, Yongsheng Liu, 2012, Biochimica et biophysica acta.

Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.

B. Sykes, L. Fliegel, J. Rainey, 2006, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.

B D Sykes, B. Sykes, P. Mercier, 2000, Biochemistry.

VADAR: a web server for quantitative evaluation of protein structure quality

David S. Wishart, Haiyan Zhang, Leigh Willard, 2003, Nucleic Acids Res..

Spin-echo 1H NMR studies of differential mobility in gizzard myosin and its subfragments.

B. Sykes, D. Hartshorne, L. E. Sommerville, 1990, Biochemistry.

Energetics and kinetics of interconversion of two myosin subfragment-1.adenosine 5'-diphosphate complexes as viewed by phosphorus-31 nuclear magnetic resonance.

B D Sykes, B. Sykes, J. Shriver, 1981, Biochemistry.

Phosphorus-31 nuclear magnetic resonance evidence for two conformations of myosin subfragment-1.nucleotide complexes.

B D Sykes, B. Sykes, J. Shriver, 1981, Biochemistry.

Effects of manganous ion on the phosphorus-31 nuclear magnetic resonance spectrum of adenosine triphosphate bound to nitrated G-actin: proximity of divalent metal ion and nucleotide binding sites.

B. Sykes, M. Brauer, 1982, Biochemistry.

Energetics of the equilibrium between two nucleotide-free myosin subfragment 1 states using fluorine-19 nuclear magnetic resonance.

B. Sykes, J. Shriver, 1982, Biochemistry.

DNA Binding: a Novel Function of Pseudomonas aeruginosa Type IV Pili

Brian D Sykes, B. Sykes, C. Slupsky, 2005, Journal of bacteriology.

Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.

R. Hodges, B. Sykes, G. Shaw, 1991, Biochemistry.

A 1H NMR determination of the solution conformation of a synthetic peptide analogue of calcium-binding site III of rabbit skeletal troponin C.

R. Hodges, B. Sykes, B. Marsden, 1989, Biochemistry.

1H-NMR studies of synthetic peptide analogues of calcium-binding site III of rabbit skeletal troponin C: effect on the lanthanum affinity of the interchange of aspartic acid and asparagine residues at the metal ion coordinating positions.

B D Sykes, R. Hodges, B. Sykes, 1988, Biochemistry.

Growth factor receptors: structure, mechanism, and drug discovery.

B. Sykes, C. McInnes, Campbell McInnes, 1997, Biopolymers.

Injury and protection in split-thickness skin after very rapid cooling and warming.

B. Sykes, E. Tredget, L. Mcgann, 1997, Cryobiology.

Structure/function of human herpesvirus‐8 MIP‐II (1–71) and the antagonist N‐terminal segment (1–10)

B. Sykes, J. Gong, M. Crump, 2001, FEBS letters.

Metagenomic and metabolomic characterization of rabies encephalitis: new insights into the treatment of an ancient disease.

R. Holt, B. Sykes, C. Slupsky, 2013, The Journal of infectious diseases.

The PAX3 and 7 homeodomains have evolved unique determinants that influence DNA-binding, structure and communication with the paired domain

B. Sykes, D. Underhill, Gareth N. Corry, 2019, bioRxiv.

Divergence of PAX 3 and PAX 7 DNA-binding 1 The PAX

B. Sykes, D. Underhill, Gareth N. Corry, 2019 .

The metabolomics of asthma: novel diagnostic potential.

B. Sykes, B. Rowe, D. Adamko, 2012, Chest.

Diagnostic Potential The Metabolomics of Asthma : Novel

B. Sykes, B. Rowe, D. Adamko, 2012 .

Differential Binding of Desmopressin and Vasopressin to Neurophysin-II*

B. Sykes, E. Breslow, Jianjun Wang, 1996, The Journal of Biological Chemistry.

NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor.

B. Sykes, M. O’Connor-McCourt, C. McInnes, 2000, Protein engineering.

Structure-function relationships in spruce budworm antifreeze protein revealed by isoform diversity.

B. Sykes, S. Graether, P. Davies, 2000, European journal of biochemistry.

A new paradigm for fish antifreeze protein binding to ice

R. Hodges, B. Sykes, C. Kay, 2002 .

Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.

B. Sykes, S. Graether, M. Daley, 2004, Biochemistry.

Cold survival in freeze‐intolerant insects

B. Sykes, S. Graether, 2004 .

The structure and function of b-helical antifreeze proteins

B. Sykes, S. Graether, 2004 .

Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins.

B. Sykes, S. Graether, 2004, European journal of biochemistry.

Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature.

B. Sykes, L. Spyracopoulos, Z. Jia, 2003, Journal of molecular biology.

NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures.

W. Gronwald, B. Sykes, P. Davies, 1996, Biochemistry.

Structure and dynamics of a beta-helical antifreeze protein.

B. Sykes, L. Spyracopoulos, Z. Jia, 2002, Biochemistry.

Structure and Dynamics of a -Helical Antifreeze Protein ,

B. Sykes, L. Spyracopoulos, Z. Jia, 2002 .

Effect of a mutation on the structure and dynamics of an α‐helical antifreeze protein in water and ice

B. Sykes, C. Slupsky, S. Graether, 2006, Proteins.

Identification of the ice‐binding face of antifreeze protein from Tenebrio molitor

B. Sykes, P. Davies, C. Marshall, 2002, FEBS letters.

Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function.

B D Sykes, B Dewald, B. Sykes, 1999, Biochemistry.

Characterization of Transforming Growth Factor Alpha binding to Epidermal Growth Factor receptor through NMR structure determination and NOE analysis methods

D. Hoyt, B. Sykes, C. McInnes, 2002 .

NMR Study of the Transforming Growth Factor-α (TGF-α)-Epidermal Growth Factor Receptor Complex

D. Hoyt, B. Sykes, M. O’Connor-McCourt, 1996, The Journal of Biological Chemistry.

Interaction of transforming growth factor alpha with the epidermal growth factor receptor: binding kinetics and differential mobility within the bound TGF-alpha.

D. Hoyt, B. Sykes, M. O’Connor-McCourt, 1994, Biochemistry.

A PagP fusion protein system for the expression of intrinsically disordered proteins in Escherichia coli.

B. Sykes, P. Hwang, Jonathan S Pan, 2012, Protein expression and purification.

Neutrophil activation by monomeric interleukin-8

B. Sykes, K. Rajarathnam, C. Kay, 1994 .

Effects of Phe‐to‐Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies

B. Sykes, P. Mercier, Xu Wang, 2005, Protein science : a publication of the Protein Society.

Structure Determination by NMR

B. Sykes, D. Corson, Monica X. Li, 2002 .

Nuclear magnetic resonance studies of CXC chemokine receptor 4 allosteric peptide agonists in solution

B. Sykes, J. Rainey, O. Baryshnikova, 2006 .

Lipid-bound Structure of an Apolipoprotein E-derived Peptide*

B. Sykes, C. Slupsky, V. Raussens, 2003, Journal of Biological Chemistry.

NMR Structure and Dynamics of a Receptor-active Apolipoprotein E Peptide*

B. Sykes, C. Slupsky, V. Raussens, 2002, The Journal of Biological Chemistry.

Metabolomic study of disease progression in scrapie prion infected mice; validation of a novel method for brain metabolite extraction

B. Sykes, D. Westaway, P. Mercier, 2020, Metabolomics.

Caenorhabditis elegans diet significantly affects metabolic profile, mitochondrial DNA levels, lifespan and brood size.

B. Sykes, X. Hu, S. Reinke, 2010, Molecular genetics and metabolism.

Insight into Lipid Surface Recognition and Reversible Conformational Adaptations of an Exchangeable Apolipoprotein by Multidimensional Heteronuclear NMR Techniques*

B. Sykes, S. Gagné, R. Ryan, 1997, The Journal of Biological Chemistry.

Structure‐activity relationships of chemokines

B. Sykes, K. Rajarathnam, B. Dewald, 1995, Journal of leukocyte biology.

The carboxyl-terminal segment of apolipoprotein A-V undergoes a lipid-induced conformational change.

B. Sykes, R. Ryan, Brian L. Lee, 2010, Biochemistry.

Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies.

D. Wishart, B. Sykes, E. Pai, 2011, Biochemistry.

Monitoring Prion Protein Stability by NMR

B. Sykes, S. Graether, O. Julien, 2009, Journal of toxicology and environmental health. Part A.

Structures of the troponin C regulatory domains in the apo and calcium-saturated states

B. Sykes, S. Tsuda, S. Gagné, 1995, Nature Structural Biology.

Drugging the Sarcomere, a Delicate Balance: Position of N-Terminal Charge of the Inhibitor W7.

B. Sykes, T. Kampourakis, F. Cai, 2022, ACS chemical biology.

Correlating structure, dynamics, and function in transmembrane segment VII of the Na+/H+ exchanger isoform 1.

B. Sykes, L. Fliegel, T. Reddy, 2010, Biochimica et biophysica acta.

The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I.

I. M. Robertson, B. Sykes, P. Mercier, 2008, Biochemistry.

Probing nascent structures in peptides using natural abundance 13C NMR relaxation and reduced spectral density mapping

B. Sykes, L. Spyracopoulos, C. Slupsky, 2007, Proteins.

Backbone dynamics of SDF‐1α determined by NMR: Interpretation in the presence of monomer–dimer equilibrium

B. Sykes, O. Baryshnikova, 2006, Protein science : a publication of the Protein Society.

Dynamics of the C-terminal region of TnI in the troponin complex in solution.

R. Fletterick, B. Sykes, D. B. Stone, 2006, Biophysical journal.

Calcium-dependent Changes in the Flexibility of the Regulatory Domain of Troponin C in the Troponin Complex*

R. Fletterick, B. Sykes, D. B. Stone, 2005, Journal of Biological Chemistry.

Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy

B. Sykes, L. Spyracopoulos, R. Irvin, 2000, Journal of biomolecular NMR.

Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity.

L. Kay, B. Sykes, L. Spyracopoulos, 1998, Journal of molecular biology.

Effects of internal motions on the development of the two-dimensional transferred nuclear Overhauser effect

B. Sykes, A. Campbell, 1991, Journal of biomolecular NMR.

Theoretical evaluation of the two-dimensional transferred nuclear overhauser effect

B. Sykes, A. Campbell, 1991 .

Correlation time adjustment factors for NOE-based structure refinement

B. Sykes, J. Baleja, 1991 .

Solution structure of phage lambda half-operator DNA by use of NMR, restrained molecular dynamics, and NOE-based refinement.

B. Sykes, J. Baleja, R. Pon, 1990, Biochemistry.

Distance measurement and structure refinement with NOE data

J. Moult, B. Sykes, J. Baleja, 1990 .

Backbone dynamics of a model membrane protein: assignment of the carbonyl carbon 13C NMR resonances in detergent-solubilized M13 coat protein.

B. Sykes, J. Weiner, G. D. Henry, 1987, Biochemistry.

Structural and functional analysis of the Na+/H+ exchanger.

B. Sykes, L. Fliegel, J. Rainey, 2007, The Biochemical journal.

Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C

Brian D Sykes, Robert F. Boyko, I. M. Robertson, 2011, Journal of biomolecular NMR.

A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids.

R. Hodges, B. Sykes, C. Kay, 1993, Biochemistry.

Calcium-induced peptide association to form an intact protein domain: 1H NMR structural evidence.

R. Hodges, B. Sykes, G. Shaw, 1990, Science.

Determination of the rotational dynamics and pH dependence of the hydrogen exchange rates of the arginine guanidino group using NMR spectroscopy

B. Sykes, G. D. Henry, 1995, Journal of Biomolecular NMR.

NMR structure of CXCR3 binding chemokine CXCL11 (ITAC)

B. Sykes, Valerie Booth, Ian Clark‐Lewis, 2004, Protein science : a publication of the Protein Society.

Unmasking ligand binding motifs: identification of a chemokine receptor motif by NMR studies of antagonist peptides.

B. Sykes, C. Slupsky, V. Booth, 2003, Journal of molecular biology.

NMR studies of active N-terminal peptides of stromal cell-derived factor-1. Structural basis for receptor binding.

B. Sykes, C. Slupsky, M. Crump, 2000, The Journal of biological chemistry.

Human CC chemokine I-309, structural consequences of the additional disulfide bond.

B. Sykes, C. Slupsky, M. Crump, 2000, Biochemistry.

Design, synthesis and characterization of a water-soluble -sheet peptide

R. Hodges, D. Wishart, B. Sykes, 1995 .

Structural analysis of the Na+/H+ exchanger isoform 1 (NHE1) using the divide and conquer approach.

B. Sykes, L. Fliegel, Brian L. Lee, 2011, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Calcium binding proteins. Elucidating the contributions to calcium affinity from an analysis of species variants and peptide fragments.

B D Sykes, B. Sykes, G. Shaw, 1990, Biochemistry and cell biology = Biochimie et biologie cellulaire.

UBC9-dependent Association between Calnexin and Protein Tyrosine Phosphatase 1B (PTP1B) at the Endoplasmic Reticulum*

B. Sykes, M. Tremblay, M. Michalak, 2015, The Journal of Biological Chemistry.

Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy

F. Richards, D. Wishart, B. Sykes, 1991, FEBS letters.

Structure of the Inhibitor W7 Bound to the Regulatory Domain of Cardiac Troponin C†

B. Sykes, Ryan M. B. Hoffman, 2009, Biochemistry.

SEQSEE: a comprehensive program suite for protein sequence analysis

David S. Wishart, Leigh Willard, Robert F. Boyko, 1994, Comput. Appl. Biosci..

Multidimensional NMR studies of an exchangeable apolipoprotein and its interactions with lipids

B. Sykes, S. Gagné, R. Ryan, 1997 .

Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C.

B D Sykes, B. Sykes, L. Spyracopoulos, 2001, Biochemistry.

Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I.

B. Sykes, P. Mercier, L. Spyracopoulos, 2001, Biochemistry.

Thermotropic phase behavior of model membranes composed of phosphatidylcholines containing dl-methyl anteisobranched fatty acids. 1. Differential scanning calorimetric and 31P NMR spectroscopic studies.

B. Sykes, R. Lewis, R. McElhaney, 1987, Biochemistry.

Neutrophil-activating Peptide-2 and Melanoma Growth-stimulatory Activity Are Functional as Monomers for Neutrophil Activation*

B. Sykes, K. Rajarathnam, C. Kay, 1997, The Journal of Biological Chemistry.

Monocyte Chemoattractant Protein-3

B. Sykes, D. Lee, D. Kwon, 2001 .

Thioimidate Bond Formation between Cardiac Troponin C and Nitrile-containing Compounds

Brittney A. Klein, I. M. Robertson, B. Sykes, 2019, ACS medicinal chemistry letters.

Probing the mechanism of cardiovascular drugs using a covalent levosimendan analog

I. M. Robertson, B. Sykes, Yin-Biao Sun, 2016, Journal of molecular and cellular cardiology.

A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA

B. Sykes, S. Reinke, D. Hockman, 2009, Nucleic acids research.

Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 1. Studies of the conformation, intrabilayer orientation, and amide hydrogen exchangeability of Ac-K2-(LA)12-K2-amide.

R. Hodges, B. Sykes, Y. Zhang, 1995, Biochemistry.

Characterization of gamma-radiation induced decomposition products of thymidine-containing dinucleoside monophosphates by nuclear magnetic resonance spectroscopy.

B. Sykes, J. Baleja, G. W. Buchko, 1993, Journal of Biomolecular Structure and Dynamics.

Versatile cardiac troponin chimera for muscle protein structural biology and drug discovery.

B. Sykes, O. Julien, Sandra E. Pineda-Sanabria, 2014, ACS chemical biology.

NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide.

B. Sykes, J. O'Neil, 1989, Biochemistry.

Optimization of NMR analysis of biological fluids for quantitative accuracy

Erik J. Saude, B. Sykes, C. Slupsky, 2006, Metabolomics.

A Molecular Basis for Different Interactions of Marine Toxins with Protein Phosphatase-1

B. Sykes, C. Holmes, J. Bagu, 1997, The Journal of Biological Chemistry.

Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: A monitor of intramolecular hydrogen bonds in helical peptides?

B. Sykes, E. Krause, F. Sönnichsen, 1996, Journal of biomolecular NMR.

Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein.

B. Sykes, G. D. Henry, 1990, Biochemistry.

Hydrogen exchange in the hydrophilic regions of detergent-solubilized M13 coat protein detected by 13C nuclear magnetic resonance isotope shifts.

B. Sykes, J. Weiner, J. O'Neil, 1986, Biophysical journal.

Nuclear magnetic resonance proton study of the aqueous chemistry of acetealdehyde and ammonia. Formation of 2,4,6-trimethyl-hexahydro-S-triazine

B. Sykes, W. Hull, B. Babior, 1973 .

Structure and dynamics of a detergent-solubilized membrane protein: measurement of amide hydrogen exchange rates in M13 coat protein by 1H NMR spectroscopy.

B. Sykes, J. O'Neil, 1988, Biochemistry.

Assignment of amide 1H and 15N NMR resonances in detergent-solubilized M13 coat protein: a model for the coat protein dimer.

B. Sykes, G. D. Henry, 1992, Biochemistry.

Characterization of quaternary structure of interleukin-8 and functional implications.

B. Sykes, K. Rajarathnam, C. Kay, 1997, Methods in enzymology.

A PROTON NUCLEAR MAGNETIC RESONANCE STUDY OF THE AQUEOUS CHEMISTRY OF ACETALDEHYDE AND AMMONIA, THE FORMATION OF 2,4,6-TRIMETHYLHEXAHYDRO-S-TRIAZINE

B. Sykes, W. Hull, B. Babior, 1973 .

Effect of trifluoroethanol on the solution structure and flexibility of desmopressin: a two-dimensional NMR study.

R. Hodges, B. Sykes, J. Wang, 2009, International journal of peptide and protein research.

Identification and localization of two distinct microenvironments for the diacylglycerol component of lipophorin particles by 13C NMR.

B. Sykes, R. Ryan, H. Liu, 1995, Biochemistry.

Formate can differentiate between hyperhomocysteinemia due to impaired remethylation and impaired transsulfuration.

B. Sykes, M. Brosnan, J. Brosnan, 2012, American journal of physiology. Endocrinology and metabolism.

Structural and Functional Characterization of Transmembrane Segment VII of the Na+/H+ Exchanger Isoform 1*

B. Sykes, L. Fliegel, J. Rainey, 2006, Journal of Biological Chemistry.

Structural and Functional Characterization of Transmembrane Segment IV of the NHE1 Isoform of the Na+/H+ Exchanger*

B. Sykes, D. Lindhout, L. Fliegel, 2005, Journal of Biological Chemistry.

1H NMR spectroscopic studies of calcium-binding proteins. 2. Histidine microenvironments in alpha- and beta-parvalbumins as determined by protonation and laser photochemically induced dynamic nuclear polarization effects.

B. Sykes, C. Kay, D. Corson, 1986, Biochemistry.

Reversible Covalent Reaction of Levosimendan with Cardiac Troponin C in Vitro and in Situ.

Brittney A. Klein, I. M. Robertson, B. Sykes, 2018, Biochemistry.

A NMR study of the interaction of N-trifluoroacetyl-D-phenylalanine with α-chymotrypsin

B. Sykes, 1968 .

Frequency-dependent phosphorus-31 nuclear magnetic resonance studies of the phosphohistidine residue to succinyl-CoA synthetase and the phosphoserine residue of glycogen phosphorylase a.

H. Vogel, B. Sykes, W. A. Bridger, 1982, Biochemistry.

Calcium-binding proteins: calcium(II)-lanthanide(III) exchange in carp parvalbumin

B. Sykes, D. Corson, T. C. Williams, 1984 .

Structure of trans-resveratrol in complex with the cardiac regulatory protein troponin C.

I. M. Robertson, B. Sykes, Sandra E. Pineda-Sanabria, 2011, Biochemistry.

Phosphorylation and mutation of human cardiac troponin I deferentially destabilize the interaction of the functional regions of troponin I with troponin C.

B. Sykes, J. V. Van Eyk, D. Lindhout, 2003, Biochemistry.

19F nuclear magnetic resonance studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. Orientational order in the presence of a series of positional isomers of cis-octadecenoic acid.

B. Sykes, F. Gunstone, R. McElhaney, 1985, Biochemistry.

Methods to study membrane protein structure in solution.

B. Sykes, G. D. Henry, Gillian D. Henry, 1994, Methods in enzymology.

Differential stability of the bovine prion protein upon urea unfolding

B. Sykes, S. Chatterjee, S. Graether, 2009, Protein science : a publication of the Protein Society.

Mutations in the Saccharomyces cerevisiae succinate dehydrogenase result in distinct metabolic phenotypes revealed through (1)H NMR-based metabolic footprinting.

B. Sykes, S. Szeto, S. Reinke, 2010, Journal of proteome research.

Tryptophan side chain conformers monitored by NMR and time‐resolved fluorescence spectroscopies

B. Sykes, Guoli Wang, Y. Engelborghs, 2012, Proteins.

The Role of Electrostatics in the Mechanism of Cardiac Thin Filament Based Sensitizers.

Brittney A. Klein, I. M. Robertson, B. Sykes, 2020, ACS chemical biology.

Detergent-solubilized M13 coat protein exists as an asymmetric dimer. Observation of individual monomers by 15N, 13C and 1H nuclear magnetic resonance spectroscopy.

B. Sykes, G. D. Henry, 1990, Journal of Molecular Biology.

Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides

B. Sykes, R. Campbell, A. Chakrabartty, 2007, BMC Structural Biology.

Unusual β-sheet periodicity in small cyclic peptides

David S. Wishart, Wolfram Gronwald, Brian D. Sykes, 1998, Nature Structural Biology.

Peptide destabilization by two adjacent D-amino acids in single-stranded amphipathic alpha-helices.

R. Hodges, B. Sykes, E. Krause, 1996, Peptide research.

Metabolomic profiling of asthma: diagnostic utility of urine nuclear magnetic resonance spectroscopy.

Erik J. Saude, B. Sykes, B. Rowe, 2011, The Journal of allergy and clinical immunology.

Dynamics of Cryoprotectant Permeation in Porcine Heart Valve Leaflets

B. Sykes, C. Slupsky, J. Lakey, 2003, Cell transplantation.

Structural and functional analysis of critical amino acids in TMVI of the NHE1 isoform of the Na+/H+ exchanger.

B. Sykes, L. Fliegel, Brian L. Lee, 2011, Biochimica et biophysica acta.

Biochemical structure determination by NMR

B. Sykes, J. Glickson, A. Bothner‐By, 1982 .

Relaxation of individual transitions in an AX spectrum. Use of interference terms to separate the dipolar and chemical-shift anisotropy contributions to the relaxation of 31P and 19F nuclei in macromolecules

S. Withers, N. Madsen, B. Sykes, 1985 .

19F nuclear magnetic resonance studies of selectively fluorinated derivatives of G- and F-actin.

B. Sykes, M. Brauer, 1986, Biochemistry.

Structural Changes Induced by the Binding of the Calcium Desensitizer W7 to Cardiac Troponin.

B. Sykes, P. Hwang, F. Cai, 2018, Biochemistry.

Solution Structure of Human Cardiac Troponin C in Complex with the Green Tea Polyphenol, (−)-Epigallocatechin 3-Gallate*

I. M. Robertson, B. Sykes, Monica X. Li, 2009, The Journal of Biological Chemistry.

Thermodynamic insights into proteins from NMR spin relaxation studies.

B. Sykes, L. Spyracopoulos, 2001, Current opinion in structural biology.

A 19F and 1H goniometric split-millicoil NMR probe for solid-state NMR†

B. Sykes, Jeffrey S Devries, Xingang Zhao, 2007 .

High-throughput, multi-platform metabolomics on very small volumes: 1H NMR metabolite identification in an unadulterated tube-in-tube system

B. Sykes, P. Mercier, R. Fahlman, 2014, Metabolomics.

1H nuclear magnetic resonance study of the two calcium-binding sites of porcine intestinal calcium-binding protein.

B. Sykes, J. Shelling, 1985, The Journal of biological chemistry.

Design of stopped‐flow NMR rapid‐mixing cells

B. Sykes, J. J. Grimaldi, 1975 .

Construction of transforming growth factor alpha (TGF-alpha) phage library and identification of high binders of epidermal growth factor receptor (EGFR) by phage display.

D. Hoyt, B. Sykes, M. O’Connor-McCourt, 1997, Journal of biochemistry.

The Human inheritance : genes, language, and evolution

B. Sykes, 1999 .

Nuclear magnetic resonance determination of metal-proton distances in a synthetic calcium binding site of rabbit skeletal troponin C.

I. Kuntz, R. Hodges, L. Kay, 1985, Biochemistry.

NMR solution structure of calcium-saturated skeletal muscle troponin C.

B D Sykes, B. Sykes, C. Slupsky, 1995, Biochemistry.

Semisynthesis and segmental isotope labeling of the apoE3 N-terminal domain using expressed protein ligation

B. Sykes, V. Raussens, P. Weers, 2009, Journal of Lipid Research.

THE DETECTION OF SUBSTRATE DISTORTION BY LYSOZYME: AN APPLICATION OF NMR TO THE STUDY OF ENZYME SUBSTRATE REACTIONS *

B. Sykes, S. Patt, D. Dolphin, 1973, Annals of the New York Academy of Sciences.

20 – The nmr Detection of the Distorted Intermediate in the Lysozyme Catalyzed Cleavage of Cell Wall Tetrasaccharide

B. Sykes, S. Patt, D. Dolphin, 1974 .

The role of distortion in the lysozyme mechanism.

B. Sykes, S. Patt, D. Dolphin, 1972, Cold Spring Harbor symposia on quantitative biology.

A nuclear magnetic resonance study of lysozyme inhibition. Effects of dimerization and pH on saccharide binding.

B. Sykes, J. Studebaker, R. Wien, 1971, Journal of the American Chemical Society.

Sykes, Brian D.: When Biochemistry became Chemistry

B. Sykes, 2007 .

Aspartate transcarbamylase. A study by transient nuclear magnetic resonance of the binding of succinate to the native enzyme and its catalytic subunit.

B. Sykes, G. Stark, P. Schmidt, 1970, The Journal of biological chemistry.

A nuclear magnetic resonance study of the binding of substrate analogues to a modified aspartate transcarbamylase.

B. Sykes, D. Evans, C. McMurray, 1972, Biochemical and biophysical research communications.

Conformational differences between cis and trans proline isomers of a peptide antigen representing the receptor binding domain of Pseudomonas aeruginosa as studied by 1H‐nmr

R. Hodges, B. Sykes, C. Kay, 1994, Biopolymers.

The Role of Transient Changes in Sample Susceptibility in Causing Apparent Multiple-Quantum Peaks in HOESY Spectra

B. Sykes, F. Sönnichsen, B. Lix, 1996 .

Structure of the C-domain of Human Cardiac Troponin C in Complex with the Ca2+ Sensitizing Drug EMD 57033*

B. Sykes, L. Spyracopoulos, R. Solaro, 2001, The Journal of Biological Chemistry.

Using lanthanide ions to align troponin complexes in solution: Order of lanthanide occupancy in cardiac troponin C

B. Sykes, D. Lindhout, G. Gay, 2004, Protein science : a publication of the Protein Society.

Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy

Brian D. Sykes, Erik J. Saude, B. Sykes, 2002, European Biophysics Journal.

Diverse residues of intracellular loop 5 of the Na+/H+ exchanger modulate proton sensing, expression, activity and targeting.

Ka Yee Wong, B. Sykes, R. McKay, 2019, Biochimica et biophysica acta. Biomembranes.

Structural and functional analysis of the transmembrane segment pair VI and VII of the NHE1 isoform of the Na+/H+ exchanger.

B. Sykes, L. Fliegel, Brian L. Lee, 2014, Biochemistry.

StructuralandFunctionalCharacterizationofTransmembrane SegmentIXoftheNHE1IsoformoftheNa/HExchanger *

B. Sykes, L. Fliegel, T. Reddy, 2008 .

Interaction of Actin 1–28 with Myosin and Troponin I and the Importance of These Interactions to Muscle Regulation

R. Hodges, B. Sykes, F. Sönnichsen, 1991 .

Mass Incarceration and the Underground Economy in America

B. Sykes, A. Geller, 2017 .

On the Use of NMR in Complex Biological Systems: NMR Studies of Calcium Sensitive Interactions amongst Muscle Proteins

D. Wishart, B. Sykes, C. Slupsky, 1996 .

Calcium binding proteins: optical stopped-flow and proton nuclear magnetic resonance studies of the binding of the lanthanide series of metal ions to parvalbumin.

B. Sykes, D. Corson, T. C. Williams, 1983, Biochemistry.

A determination of the relative compactness of the Ca2+‐binding sites of a Ca2+‐binding fragment of troponin‐c and parvalbumin using lanthanide‐induced 1H NMR shifts

E. R. Birnbaum, B. Sykes, Lana Lee, 1979, FEBS letters.

1H NMR solution structure of an active monomeric interleukin-8.

B D Sykes, B. Sykes, K. Rajarathnam, 1995, Biochemistry.

Fluorine-19 NMR studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. Fluorine-19 NMR line shape and orientational order in the gel state

B. Sykes, R. McElhaney, P. Macdonald, 1984 .

CAMRA: Chemical shift based computer aided protein NMR assignments

Robert F. Boyko, B D Sykes, W. Gronwald, 1998, Journal of biomolecular NMR.

Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein

B. Sykes, R. Ryan, Jianjun Wang, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Gas-phase memory of solution-phase protein conformation: H/D exchange and Fourier transform ion cyclotron resonance mass spectrometry of the N-terminal domain of cardiac troponin C

Michael A. Freitas, B. Sykes, Fang Wang, 1999 .

PJNMR: a platform-independent graphical simulation tool for NMR spectroscopy.

Paul-Jean Letourneau, Robert Boyko, Brian D Sykes, 2003, Journal of magnetic resonance.

Automated 1H and 13C chemical shift prediction using the BioMagResBank

Robert F. Boyko, B D Sykes, D. Wishart, 1997, Journal of biomolecular NMR.

Metabolomic profiling in multiple sclerosis: insights into biomarkers and pathogenesis

B. Sykes, D. Broadhurst, C. Power, 2014, Multiple sclerosis.

Fluorine-19 nuclear magnetic resonance studies of lipid fatty acyl chain order and dynamics in Acholeplasma laidlawii B membranes. A physical, biochemical, and biological evaluation of monofluoropalmitic acids as membrane probes.

B. Sykes, R. McElhaney, P. Macdonald, 1983, Biochemistry.

Computer‐Aided Drug Discovery Approach Finds Calcium Sensitizer of Cardiac Troponin

J. Mccammon, B. Sykes, S. Lindert, 2015, Chemical biology & drug design.

Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregation.

D. Wishart, B. Sykes, T. Bjorndahl, 2018, Biochimica et biophysica acta. Proteins and proteomics.

Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.

R. Hodges, B. Sykes, G. Shaw, 1993, Biochemistry.

1H NMR evidence that Glu‐38 interacts with the N‐terminal functional domain in interleukin‐8

B. Sykes, K. Rajarathnam, B. Dewald, 1996, FEBS letters.

Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy.

B. Sykes, K. Kim, I. Clark‐Lewis, 1995, The Journal of biological chemistry.

Estimation and measurement of flat or solenoidal coil inductance for radiofrequency NMR coil design.

B. Sykes, J. Rainey, Jeffrey S Devries, 2007, Journal of magnetic resonance.

Erratum to Residue-specific mobility changes in soluble oligomers of the prion protein define regions involved in aggregation, BBAPAP (2018) 982-988.

D. Wishart, B. Sykes, T. Bjorndahl, 2018, Biochimica et biophysica acta. Proteins and proteomics.

Constrained multiple sequence alignment using XALIGN

David S. Wishart, Robert F. Boyko, Brian D. Sykes, 1994, Comput. Appl. Biosci..

Is there nascent structure in the intrinsically disordered region of troponin I?

B. Sykes, P. Mercier, C. Ramos, 2011, Proteins.

An optical stopped-flow and 1H and 113Cd nuclear magnetic resonance study of the kinetics and stoichiometry of the interaction of the lanthanide Yb3+ with carp parvalbumin.

B. Sykes, D. Corson, L. Lee, 1983, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire.

Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C.

B. Sykes, L. Spyracopoulos, S. Tsuda, 1999, Biochemistry.

Saturation transfer of exchangeable protons in 1H-decoupled 15N INEPT spectra in water. Application to the measurement of hydrogen exchange rates in amides and proteins

B. Sykes, G. D. Henry, 1993 .

Smartnotebook: A semi-automated approach to protein sequential NMR resonance assignments

Brian D Sykes, Robert F. Boyko, B. Sykes, 2003, Journal of biomolecular NMR.

Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy.

P E Wright, B D Sykes, K Wüthrich, 1998, Journal of biomolecular NMR.

Structure-based Minimization of Transforming Growth Factor-α (TGF-α) through NMR Analysis of the Receptor-bound Ligand

B. Sykes, M. O’Connor-McCourt, C. McInnes, 1998, The Journal of Biological Chemistry.

Stopped-flow nuclear magnetic resonance spectroscopy.

B. Sykes, J. J. Grimaldi, 1978, Methods in enzymology.

Recombinant locust apolipophorin III: characterization and NMR spectroscopy.

B. Sykes, C. Kay, P. Weers, 1998, Biochimica et biophysica acta.

The two-dimensional transferred nuclear Overhauser effect: theory and practice.

B D Sykes, B. Sykes, A. Campbell, 1993, Annual review of biophysics and biomolecular structure.

Assignment of the helical structure in neuropeptide Y by HPLC studies of methionine replacement analogues and 1H-NMR spectroscopy.

B. Sykes, E. Krause, F. Sönnichsen, 1998, Biopolymers.

Metabolomic study of disease progression in scrapie prion infected mice; validation of a novel method for brain metabolite extraction

B. Sykes, D. Westaway, P. Mercier, 2020, Metabolomics.

A nuclear magnetic resonance study of the binding of acetylsalicylic acid to human serum albumin.

B. Sykes, Brian D. Sykes, 1970, Biochemical and biophysical research communications.

Structural and Functional Characterization of Transmembrane Segment IV of the NHE 1 Isoform of the Na / H Exchanger *

B. Sykes, D. Lindhout, L. Fliegel, 2005 .

Interaction between the regulatory domain of cardiac troponin C and the acidosis-resistant cardiac troponin I A162H.

I. M. Robertson, B. Sykes, Monica X. Li, 2013, Cardiovascular research.

Elucidation of Isoform-dependent pH Sensitivity of Troponin I by NMR Spectroscopy*

I. M. Robertson, B. Sykes, Monica X. Li, 2011, The Journal of Biological Chemistry.

1H NMR derived metabolomic profile of neonatal asphyxia in umbilical cord serum: implications for hypoxic ischemic encephalopathy.

B. Sykes, G. Boylan, D. Broadhurst, 2013, Journal of proteome research.

Saxons, Vikings, and Celts: The Genetic Roots of Britain and Ireland

B. Sykes, 2006 .

NMR solution structure of the receptor binding domain of Pseudomonas aeruginosa pilin strain P1. Identification of a β‐turn

R. Hodges, B. Sykes, H. Sheth, 2009 .

The role of side chain conformational flexibility in surface recognition by Tenebrio molitor antifreeze protein

B. Sykes, M. Daley, 2003, Protein science : a publication of the Protein Society.

Solution conformation of an immunogenic peptide derived from the principal neutralizing determinant of the HIV-2 envelope glycoprotein gp125.

H. Dyson, B. Sykes, N. Assa‐Munt, 1996, Folding & design.

1H-NMR evidence for two buried ASN side-chains in the c-Myc-Max heterodimeric α-helical coiled-coil

R. Hodges, B. Sykes, C. Kay, 1997 .

Biophysical studies on the calcium trigger of muscle contraction

B. Sykes, C. Kay, W. Mccubbin, 1987, Biopolymers.

Differential stability of the bovine prion protein upon urea unfolding

B. Sykes, S. Chatterjee, S. Graether, 2009, Protein science : a publication of the Protein Society.

Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.

R. Hodges, B. Sykes, G. Shaw, 1993, Biochemistry.

Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides

B. Sykes, R. Campbell, A. Chakrabartty, 2007, BMC Structural Biology.

THE EVALUATION OF ISOTOPE EDITING AND FILTERING FOR PROTEIN-LIGAND INTERACTION ELUCIDATION BY NMR

I. M. Robertson, B. Sykes, L. Spyracopoulos, 2009 .

Letter to the Editor: Complete 1H, 13C and 15N backbone assignments for the hepatitis A virus 3C protease

D. Wishart, B. Sykes, L. Spyracopoulos, 2001, Journal of biomolecular NMR.

Assignment and characterization of the histidine resonances in the 1H nuclear magnetic resonance spectra of rabbit tropomyosins.

B. Sykes, B. Edwards, 1978, Biochemistry.

Dna Binding: a Novel Function Of

B. Sykes, C. Slupsky, R. Irvin, 2005 .

Rapid anisotropic motion of the Ca2+-transport ATPase of the rabbit skeletal muscle sarcoplasmic reticulum.

B. Sykes, B. A. Manuck, 1977, Canadian journal of biochemistry.

Structures reveal details of small molecule binding to cardiac troponin.

B. Sykes, S. Lindert, F. West, 2016, Journal of molecular and cellular cardiology.

Structural and functional analysis of extracellular loop 2 of the Na(+)/H(+) exchanger.

B. Sykes, L. Fliegel, Yongsheng Liu, 2009, Biochimica et biophysica acta.

Structural Basis of Tirasemtiv Activation of Fast Skeletal Muscle.

B. Sykes, P. Mercier, J. Hartman, 2021, Journal of medicinal chemistry.

Structural and Functional Characterization of Transmembrane Segment IX of the NHE1 Isoform of the Na+/H+ Exchanger*

B. Sykes, L. Fliegel, T. Reddy, 2008, Journal of Biological Chemistry.

Internal pH indicators for biomolecular NMR

B. Sykes, T. C. Williams, O. Baryshnikova, 2008, Journal of biomolecular NMR.

Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies.

D. Wishart, B. Sykes, E. Pai, 2011, Biochemistry.

Bmc Structural Biology Metal Ion-dependent, Reversible, Protein Filament Formation by Designed Beta-roll Polypeptides

B. Sykes, R. Campbell, A. Chakrabartty, 2022 .

13C and chemical shift referencing in biomolecular NMR

D. Wishart, H. Dyson, E. Oldfield, 1995 .

The metabolomics of asthma: novel diagnostic potential.

B. Sykes, B. Rowe, D. Adamko, 2012, Chest.

Dynamics of cryoprotectant permeation in porcine heart valve leaflets.

B. Sykes, C. Slupsky, J. Lakey, 2003, Cell transplantation.

The role of electrostatics in the interaction of the inhibitory region of troponin I with troponin C.

Robert F. Boyko, B. Sykes, D. Lindhout, 2005, Biochemistry.

NMR evidence for a conformational adaptation of apolipophorin III upon lipid association.

B. Sykes, R. Ryan, D. Sahoo, 1998, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the apo- and calcium-saturated states.

B D Sykes, B. Sykes, L. Spyracopoulos, 1998, Biochemistry.

Conversion of a Cardiac Muscle Modulator from an Inhibitor to an Activator.

B. Sykes, T. Kampourakis, Priyanka Parijat, 2023, ACS medicinal chemistry letters.