Assessing the applicability of 19F labeled tryptophan residues to quantify protein dynamics

[1]  R. Sprangers,et al.  Observation of conformational changes that underlie the catalytic cycle of Xrn2 , 2022, Nature Chemical Biology.

[2]  K. Wüthrich,et al.  GPCR large-amplitude dynamics by 19F-NMR of aprepitant bound to the neurokinin 1 receptor , 2022, Proceedings of the National Academy of Sciences of the United States of America.

[3]  Lars V. Schäfer,et al.  How Much Entropy Is Contained in NMR Relaxation Parameters? , 2021, The journal of physical chemistry. B.

[4]  A. Gronenborn.  Small, but powerful and attractive: 19F in biomolecular NMR. , 2021, Structure.

[5]  M. Wilmanns,et al.  Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex , 2021, Nature Communications.

[6]  L. Kay,et al.  NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function , 2021, Cell.

[7]  R. Sprangers,et al.  A suite of 19F based relaxation dispersion experiments to assess biomolecular motions , 2020, Journal of Biomolecular NMR.

[8]  R. Sprangers,et al.  Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme , 2020, Proceedings of the National Academy of Sciences.

[9]  O. Mayans,et al.  What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein , 2020, Scientific Reports.

[10]  D. Nietlispach,et al.  Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor , 2020, Nature Communications.

[11]  R. Sprangers,et al.  Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems. , 2020, Progress in nuclear magnetic resonance spectroscopy.

[12]  J. Kowalska,et al.  Synthesis of Trifluoromethylated Purine Ribonucleotides and Their Evaluation as 19F NMR Probes , 2020, The Journal of organic chemistry.

[13]  R. Sprangers,et al.  Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms , 2019, Current opinion in structural biology.

[14]  Peter D Ycas,et al.  2-Fluorotyrosine is a valuable but understudied amino acid for protein-observed 19F NMR , 2019, Journal of Biomolecular NMR.

[15]  A. Gronenborn,et al.  19F NMR relaxation studies of fluorosubstituted tryptophans , 2019, Journal of Biomolecular NMR.

[16]  K. Sharp,et al.  Measuring Entropy in Molecular Recognition by Proteins. , 2018, Annual review of biophysics.

[17]  R. Sprangers,et al.  Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme , 2017, Proceedings of the National Academy of Sciences.

[18]  L. Kay,et al.  Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer , 2017, Journal of Biomolecular NMR.

[19]  R. Sprangers,et al.  The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface , 2016, RNA.

[20]  A. Vulpetti,et al.  Weak Intermolecular Hydrogen Bonds with Fluorine: Detection and Implications for Enzymatic/Chemical Reactions, Chemical Properties, and Ligand/Protein Fluorine NMR Screening. , 2016, Chemistry.

[21]  J. Rainey,et al.  Tracking Transitions in Spider Wrapping Silk Conformation and Dynamics by (19)F Nuclear Magnetic Resonance Spectroscopy. , 2016, Biochemistry.

[22]  H. Schwalbe,et al.  19F-labeling of the adenine H2-site to study large RNAs by NMR spectroscopy , 2016, Journal of biomolecular NMR.

[23]  R. Sprangers,et al.  An excess of catalytically required motions inhibits the scavenger decapping enzyme , 2015, Nature chemical biology.

[24]  T. S. Kobilka,et al.  Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling , 2015, Cell.

[25]  A. Manglik,et al.  A comparison of chemical shift sensitivity of trifluoromethyl tags: optimizing resolution in 19F NMR studies of proteins , 2015, Journal of biomolecular NMR.

[26]  A. Mittermaier,et al.  Relaxation dispersion NMR spectroscopy for the study of protein allostery , 2015, Biophysical Reviews.

[27]  R. Prosser,et al.  Conformational selection and functional dynamics of calmodulin: a (19)F nuclear magnetic resonance study. , 2014, Biochemistry.

[28]  A. Baldwin.  An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange , 2014, Journal of magnetic resonance.

[29]  G. Montelione,et al.  (19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus. , 2014, Structure.

[30]  K. Wüthrich,et al.  Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs. , 2013, Current opinion in structural biology.

[31]  K. Sharp,et al.  Microscopic insights into the NMR relaxation-based protein conformational entropy meter. , 2013, Journal of the American Chemical Society.

[32]  R. Sprangers,et al.  The Archaeal Exosome: Identification and Quantification of Site-Specific Motions That Correlate with Cap and RNA Binding** , 2013, Angewandte Chemie.

[33]  R. Dror,et al.  The role of ligands on the equilibria between functional states of a G protein-coupled receptor. , 2013, Journal of the American Chemical Society.

[34]  R. Konrat,et al.  Allosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic Core , 2013, ACS chemical biology.

[35]  Ciara Kyne,et al.  Simple and inexpensive incorporation of 19F-tryptophan for protein NMR spectroscopy. , 2012, Chemical communications.

[36]  A. Wlodawer,et al.  Specific fluorine labeling of the HyHEL10 antibody affects antigen binding and dynamics. , 2012, Biochemistry.

[37]  T. Mak,et al.  Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment , 2012, Proceedings of the National Academy of Sciences.

[38]  R. Prosser,et al.  Current applications of 19F NMR to studies of protein structure and dynamics. , 2012, Progress in nuclear magnetic resonance spectroscopy.

[39]  Kurt Wüthrich,et al.  Biased Signaling Pathways in β2-Adrenergic Receptor Characterized by 19F-NMR , 2012, Science.

[40]  S. Floor,et al.  Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan , 2012, Proceedings of the National Academy of Sciences.

[41]  K. Kloiber,et al.  Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy , 2011, Journal of biomolecular NMR.

[42]  C. Tian,et al.  Site‐specific 19F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid , 2011, Protein science : a publication of the Protein Society.

[43]  R. Micura,et al.  5-Fluoro pyrimidines: labels to probe DNA and RNA secondary structures by 1D 19F NMR spectroscopy , 2009, Nucleic acids research.

[44]  Paul Schanda,et al.  Direct observation of the dynamic process underlying allosteric signal transmission. , 2009, Journal of the American Chemical Society.

[45]  R. Parker,et al.  Structural basis of dcp2 recognition and activation by dcp1. , 2008, Molecular cell.

[46]  D. Kern,et al.  Dynamic personalities of proteins , 2007, Nature.

[47]  L. Scott,et al.  Synthesis of 5-fluoropyrimidine nucleotides as sensitive NMR probes of RNA structure. , 2007, Journal of the American Chemical Society.

[48]  Lewis E. Kay,et al.  Quantitative dynamics and binding studies of the 20S proteasome by NMR , 2007, Nature.

[49]  R. Mehl,et al.  Site-specific incorporation of a (19)F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity. , 2007, Journal of the American Chemical Society.

[50]  Timothy D. Craggs,et al.  19F NMR studies of the native and denatured states of green fluorescent protein. , 2006, Journal of the American Chemical Society.

[51]  Francesca Massi,et al.  Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. , 2006, Chemical reviews.

[52]  P. Schanda,et al.  Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. , 2006, Journal of magnetic resonance.

[53]  Walid A Houry,et al.  Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[54]  A. Palmer,et al.  NMR characterization of the dynamics of biomacromolecules. , 2004, Chemical reviews.

[55]  L. Kay,et al.  Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. , 2003, Journal of the American Chemical Society.

[56]  J. Pinkner,et al.  Real-time and equilibrium 19F-NMR studies reveal the role of domain–domain interactions in the folding of the chaperone PapD , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[57]  J. T. Gerig,et al.  Origins of Fluorine NMR Chemical Shifts in Fluorine-Containing Proteins† , 2000 .

[58]  R. Huber,et al.  Atomic mutations at the single tryptophan residue of human recombinant annexin V: effects on structure, stability, and activity. , 1999, Biochemistry.

[59]  G. Gilliland,et al.  Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine. , 1998, Journal of molecular biology.

[60]  R. Furter.  Expansion of the genetic code: Site‐directed p‐fluoro‐phenylalanine incorporation in Escherichia coli , 1998, Protein science : a publication of the Protein Society.

[61]  B. Sykes,et al.  Fluorotyrosine alkaline phosphatase. 19F nuclear magnetic resonance relaxation times and molecular motion of the individual fluorotyrosines. , 1974, Biochemistry.