J. Boyd

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A refined solution structure of hen lysozyme determined using residual dipolar coupling data

C. Dobson, H. Schwalbe, L. J. Smith, 2001, Protein science : a publication of the Protein Society.

Observation of carbon labelling in cell metabolites using proton spin echo NMR.

I. Campbell, K. Brindle, J. Boyd, 1982, Biochemical and biophysical research communications.

The C1q receptor site on immunoglobulin G

D. Burton, R. Dwek, J. Novotný, 1980, Nature.

New methods for measurement of long-range proton-carbon coupling constants in oligosaccharides

R. Dwek, D. Uhrín, M. Wormald, 1992 .

Specific operator manipulations of heteronuclear scalar-coupled spin systems using phase-modulated selective waveforms

J. Boyd, N. Soffe, T. Norwood, 1991 .

Structural determinants of protein dynamics: analysis of 15N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme.

C. Dobson, M. Buck, D. Mackenzie, 1995, Biochemistry.

Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae.

R. J. Williams, G. Pielak, J. Boyd, 1991, Biochemistry.

Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c.

R. J. Williams, G. Pielak, J. Boyd, 1990, Biochemistry.

The solution conformations of the subclasses of human IgG deduced from sedimentation and small angle X-ray scattering studies.

D. Burton, C. Nave, R. Jefferis, 1987, Molecular immunology.

Correlation of proton chemical shifts in proteins using two-dimensional exchange correlated spectroscopy

G. Moore, J. Boyd, Glyn Williams, 1984 .

Conformational transitions in N-linked oligosaccharides.

W. Richards, R. Dwek, T. Rademacher, 1986, Biochemistry.

Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts.

R. J. Williams, G. Pielak, J. Boyd, 1991, Biochemistry.

One-Dimensional Inverse-Detected Methods for Measurement of Long-Range Proton-Carbon Coupling Constants. Application to Saccharides

R. Dwek, A. Mele, K. Kövér, 1994 .

Interaction of saccharide haptens with myeloma proteins. A 270-MHz proton nuclear magnetic resonance study.

R. Dwek, J. Boyd, P. Gettins, 1981, Biochemistry.

A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange

I. Campbell, G. Radda, K. Brindle, 1984 .

Cool Decoupling and Mixing Wave-Forms

I. Campbell, E. Kupče, J. Boyd, 1994 .

The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions

Jonathan Boyd, Iain D. Campbell, I. Campbell, 1992, Cell.

A method for the rapid assignment of 1H NMR spectra of oligosaccharides using homonuclear Hartmann-Hahn spectroscopy.

R. Dwek, T. Rademacher, S. Homans, 1987, Proceedings of the National Academy of Sciences of the United States of America.

A heteronuclear NMR study

G. Panayotou, M. Waterfield, J. Boyd, 2002 .

Analysis of cross peak fine structure in multiple-quantum filtered COSY spectra

C. Redfield, J. Boyd, 1986 .

Identification of glycine spin systems in 1H NMR spectra of proteins using multiple quantum coherences

C. Dobson, C. Redfield, J. Boyd, 1985, FEBS letters.

The application of a simple analog phase-shifting device in multiple-quantum NMR

C. Redfield, J. Boyd, R. Porteous, 1985 .

Correlation of proton chemical shifts in proteins using two-dimensional double-quantum spectroscopy

C. Dobson, C. Redfield, J. Boyd, 1983 .

Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c family.

R. J. Williams, G. Moore, G. Pielak, 1988, European journal of biochemistry.

The Construction of a High-Resolution 750 MHz Probehead

J. Boyd, N. Soffe, M. Leonard, 1995 .

Mobility and symmetry in the Fc and pFc' fragments as probed by 1H NMR.

R. Dwek, P. Závodszky, J. Boyd, 1979, Molecular immunology.

Assignment of resonances in the 1H NMR spectrum of human lysozyme.

C. Dobson, C. Redfield, J. Boyd, 1985, European journal of biochemistry.

The generation of phase-sensitive 2D 15N1H spectra using gradient pulses for coherence-transfer-pathway selection

R. Hurd, J. Boyd, D. Plant, 1992 .

Hydrogen bonding in steroidogenesis: studies on new heterocyclic analogs of estrone that inhibit human estradiol 17 beta-dehydrogenase.

J. Boyd, F. Sweet, Ó. Medina, 1991, Biochemical and biophysical research communications.

Short selective pulses for biochemical applications.

I. Campbell, E. Kupče, J. Boyd, 1995, Journal of magnetic resonance. Series B.

New NMR technique for determining long-range heteronuclear proton-nitrogen-15 correlations in proteins

I. Campbell, J. Boyd, N. Soffe, 1990 .

Selective excitation by pulse shaping combined with phase modulation

J. Boyd, N. Soffe, 1989 .

Measurement of 15N Relaxation Data from the Side Chains of Asparagine and Glutamine Residues in Proteins

J. Boyd, 1995 .

The hairpin structure of the 6F11F22F2 fragment from human fibronectin enhances gelatin binding

Jonathan Boyd, I. Campbell, D. Staunton, 2001, The EMBO journal.

1H- and 13C-n.m.r. assignments and conformational analysis of some monosaccharide and oligosaccharide substrate-analogues of lysozyme.

M. Delepierre, R. Porteous, J. Boyd, 1985, Carbohydrate research.

Comparison of techniques for 1H-detected heteronuclear 1H15N Spectroscopy

I. Campbell, J. Boyd, N. Soffe, 1990 .

140 H/D isotopomers identified by long-range NMR hyperfine shifts in ruthenium(III) ammine complexes. Hyperconjugation in Ru-NH3 bonding.

J. Boyd, R. Denning, J. Harmer, 2013, Inorganic chemistry.

1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.

I. Campbell, P. Driscoll, J. Boyd, 1992, Biochemistry.

Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase

I. Campbell, G. Booker, I. Gout, 1993, Cell.

G. Barton, I. Campbell, A. Kingsman, 1994, Nature.

Human interleukin 4. The solution structure of a four-helix bundle protein.

R A Smith, C Redfield, C M Dobson, 1992, Journal of molecular biology.

Analysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques.

C. Dobson, R. Smith, C. Redfield, 1994, Journal of molecular biology.

Secondary structure and topology of human interleukin 4 in solution.

C. Dobson, R. Smith, C. Redfield, 1991, Biochemistry.

NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1

I. Campbell, F. Fogolari, A. Corazza, 2009, Journal of biomolecular NMR.

Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar ouplings

Jonathan Boyd, Lorna J. Smith, V. Higman, 2004, Journal of biomolecular NMR.

Calculation of Hypershielding Contribution to Isotropic Nitrogen Shielding in Strong Magnetic Fields.

M. B. Ferraro, M. Caputo, G. I. Pagola, 2009, Journal of chemical theory and computation.

Residual dipolar couplings and some specific models for motional averaging.

M. Deschamps, I. Campbell, J. Boyd, 2005, Journal of magnetic resonance.

Amide proton relaxation measurements employing a highly deuterated protein.

I. Campbell, T. Ulmer, J. Boyd, 2004, Journal of magnetic resonance.

The use of dipolar couplings for the structure refinement of a pair of calcium-binding EGF domains.

I. Campbell, A. Downing, J. Boyd, 2002, Methods in molecular biology.

Dynamic studies of a fibronectin type I module pair at three frequencies: Anisotropic modelling and direct determination of conformational exchange

I. Campbell, I. Phan, J. Boyd, 1996, Journal of biomolecular NMR.

Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.

R A Smith, C Redfield, C M Dobson, 1992, Biochemistry.

Influence of cross-correlation between dipolar and chemical shift anisotropy relaxation mechanisms upon the transverse relaxation rates of 15N in macromolecules

V. Krishnan, J. Boyd, U. Hommel, 1991 .

Influence of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms upon longitudinal relaxation rates of 15N in macromolecules

I. Campbell, J. Boyd, U. Hommel, 1990 .

Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.

I. Campbell, R. Cooke, M. Weir, 1992, Biochemistry.

Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy.

R. J. Williams, V. Saudek, G. Ramponi, 1989, Journal of molecular biology.

Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c.

R. J. Williams, G. Pielak, R. Atkinson, 1988, European journal of biochemistry.

Phosphopeptide binding to the N‐terminal SH2 domain of the p85α subunit of PI 3′‐kinase: A heteronuclear NMR study

I. Campbell, G. Booker, G. Panayotou, 1994, Protein science : a publication of the Protein Society.

The sequence-specific assignment of the 1H-NMR spectrum of an enzyme, horse-muscle acylphosphatase.

R. J. Williams, V. Saudek, G. Ramponi, 1989, European journal of biochemistry.

Secondary structure and backbone dynamics of human granulocyte colony-stimulating factor in solution.

I. Campbell, A. Breeze, J. Boyd, 1994, Biochemistry.

NMR at very high fields.

I. Campbell, J. Boyd, J Boyd, 1994, Structure.

Residual dipolar couplings: are multiple independent alignments always possible?

Lorna J. Smith, V. Higman, C. Redfield, 2010, Journal of biomolecular NMR.

Some NMR Experiments and a Structure Determination Employing a {15N,2H} Enriched Protein

I D Campbell, I. Campbell, S. Matthews, 1998, Journal of biomolecular NMR.

Correlation of aliphatic proton chemical shifts in proteins using two-dimensional double-quantum correlated spectroscopy

C. Dobson, J. Boyd, Christina Redfieldt, 1985 .

1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase.

I. Campbell, J. Carver, J. Boyd, 1987, Journal of molecular biology.

High-resolution 1H NMR study of the solution structure of alamethicin.

I. Campbell, J. Carver, G. Esposito, 1987, Biochemistry.

Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.

I. Campbell, G. Booker, A. Downing, 1993, Cell.

A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte.

I. Campbell, K. Brindle, J. Boyd, 1984, Biochimica et biophysica acta.

Solution structure of the LDL receptor EGF-AB pair: a paradigm for the assembly of tandem calcium binding EGF domains.

I. Campbell, P. Handford, A. Downing, 2001, Structure.

Neutron scattering studies of subcomponent C1q of first component C1 of human complement and its association with subunit C1r2C1s2 within C1.

D. Burton, R. Dwek, G. Arlaud, 1984, Journal of molecular biology.

Neutron scattering studies of the isolated C1r2C1s2 subunit of first component of human complement in solution.

D. Burton, R. Dwek, G. Arlaud, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Calculations of the contribution of ring currents to the chemical shielding anisotropy.

N. Skrynnikov, J. Boyd, 2002, Journal of the American Chemical Society.

The effects of dissolved oxygen upon amide proton relaxation and chemical shift in a perdeuterated protein.

I. Campbell, T. Ulmer, J. Boyd, 2002, Journal of magnetic resonance.

Characterization of 15N Chemical Shift Anisotropy from Orientation-Dependent Changes to 15N Chemical Shifts in Dilute Bicelle Solutions

C. Redfield, J. Boyd, 1999 .

A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c.

R. J. Williams, J. Boyd, Y. Gao, 1990, European journal of biochemistry.

Improved resolution in 1H‐detected 1H‐15N correlation experiments

I. Campbell, J. Boyd, T. Norwood, 1989, FEBS letters.

A theoretical analysis of homonuclear cross-polarization coherence transfer in liquids

R. Bazzo, J. Boyd, 1987 .

Letter to the Editor: Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1

I. Campbell, A. Corazza, G. Esposito, 2004, Journal of biomolecular NMR.

Exploring the boundaries of additivity: mixtures of NADH: quinone oxidoreductase inhibitors.

J. Boyd, A. Saksena, N. Boggs, 2011, Chemical research in toxicology.

A diagrammatic representation of both in-phase and antiphase coherence transfer processes with a simple application

I. Campbell, R. Bazzo, J. Boyd, 1987 .

Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE)

M. Deschamps, I. Campbell, J. Potts, 2005, Journal of biomolecular NMR.

Calculation of dipole-shielding polarizabilities (sigma(alphabetagamma)I): the influence of uniform electric field effects on the shielding of backbone nuclei in proteins.

C. Domene, P. Lazzeretti, C. Redfield, 2003, Journal of the American Chemical Society.

1H and 15N Hyperfine Shifts of Cytochrome c

C. Dobson, G. Pielak, J. Boyd, 1999 .