Exchangeable deuterons introduce artifacts in amide 15N CEST experiments used to study protein conformational exchange

[1]  R. Riek,et al.  15N transverse relaxation measurements for the characterization of µs–ms dynamics are deteriorated by the deuterium isotope effect on 15N resulting from solvent exchange , 2018, Journal of Biomolecular NMR.

[2]  L. Kay,et al.  Measuring Solvent Hydrogen Exchange Rates by Multifrequency Excitation 15N CEST: Application to Protein Phase Separation. , 2018, The journal of physical chemistry. B.

[3]  G. Clore,et al.  Decorrelating Kinetic and Relaxation Parameters in Exchange Saturation Transfer NMR: A Case Study of N-Terminal Huntingtin Peptides Binding to Unilamellar Lipid Vesicles. , 2018, The journal of physical chemistry. B.

[4]  L. Kay,et al.  Dramatic Decrease in CEST Measurement Times Using Multi-Site Excitation. , 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

[5]  L. Kay,et al.  Exploring methods to expedite the recording of CEST datasets using selective pulse excitation. , 2018, Journal of magnetic resonance.

[6]  A. Jerschow,et al.  Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules , 2018, Journal of Biomolecular NMR.

[7]  G. Clore,et al.  Targeting a Dark Excited State of HIV-1 Nucleocapsid by Antiretroviral Thioesters Revealed by NMR Spectroscopy. , 2018, Angewandte Chemie.

[8]  P. Vallurupalli,et al.  Measuring the signs of the methyl 1H chemical shift differences between major and ‘invisible’ minor protein conformational states using methyl 1H multi-quantum spectroscopy , 2018, Journal of Biomolecular NMR.

[9]  L. Kay,et al.  Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions , 2018, eLife.

[10]  J. Pruneda,et al.  An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1 , 2017, The EMBO journal.

[11]  L. Kay,et al.  Separating Dipolar and Chemical Exchange Magnetization Transfer Processes in 1 H-CEST. , 2017, Angewandte Chemie.

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

[13]  Woonghee Lee,et al.  NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy , 2014, Bioinform..

[14]  L. Kay,et al.  Measuring hydrogen exchange rates in invisible protein excited states , 2014, Proceedings of the National Academy of Sciences.

[15]  L. Kay,et al.  Measurement of histidine pKa values and tautomer populations in invisible protein states , 2014, Proceedings of the National Academy of Sciences.

[16]  A. Palmer,et al.  Chemical exchange in biomacromolecules: past, present, and future. , 2014, Journal of magnetic resonance.

[17]  Daiwen Yang,et al.  An off-pathway folding intermediate of an acyl carrier protein domain coexists with the folded and unfolded states under native conditions. , 2014, Angewandte Chemie.

[18]  L. Kay,et al.  Visualizing side chains of invisible protein conformers by solution NMR. , 2014, Journal of molecular biology.

[19]  Alexandar L. Hansen,et al.  Characterizing slow chemical exchange in nucleic acids by carbon CEST and low spin-lock field R(1ρ) NMR spectroscopy. , 2014, Journal of the American Chemical Society.

[20]  Peter Bachert,et al.  Chemical exchange saturation transfer (CEST) and MR Z-spectroscopy in vivo: a review of theoretical approaches and methods , 2013, Physics in medicine and biology.

[21]  L. Kay,et al.  NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers , 2013, Proceedings of the National Academy of Sciences.

[22]  Mats Carlsson,et al.  PINT: a software for integration of peak volumes and extraction of relaxation rates , 2013, Journal of Biomolecular NMR.

[23]  H. Atreya,et al.  Rapid characterization of hydrogen exchange in proteins. , 2013, Angewandte Chemie.

[24]  L. Kay,et al.  Probing slowly exchanging protein systems via 13Cα-CEST: monitoring folding of the Im7 protein , 2013, Journal of Biomolecular NMR.

[25]  L. Kay,et al.  Studying "invisible" excited protein states in slow exchange with a major state conformation. , 2012, Journal of the American Chemical Society.

[26]  Nicolas L. Fawzi,et al.  Atomic resolution dynamics on the surface of amyloid β protofibrils probed by solution NMR , 2011, Nature.

[27]  J. Forman-Kay,et al.  15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3 , 2010, Journal of Biomolecular NMR.

[28]  A. Wada,et al.  Solution structure of the E. coli ribosome hibernation promoting factor HPF: Implications for the relationship between structure and function. , 2009, Biochemical and biophysical research communications.

[29]  Brian W Matthews,et al.  Halogenated benzenes bound within a non-polar cavity in T4 lysozyme provide examples of I...S and I...Se halogen-bonding. , 2009, Journal of molecular biology.

[30]  T. Arakawa,et al.  Protein precipitation and denaturation by dimethyl sulfoxide. , 2007, Biophysical chemistry.

[31]  G. Melacini,et al.  Understanding the molecular basis for the inhibition of the Alzheimer's Abeta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy. , 2007, Journal of the American Chemical Society.

[32]  A. Palmer,et al.  Protein NMR Spectroscopy: principles and practice, 2nd ed. , 2006 .

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

[34]  D. Hansen,et al.  Determination of the geometric structure of the metal site in a blue copper protein by paramagnetic NMR. , 2006, Proceedings of the National Academy of Sciences of the United States of America.

[35]  C. Dobson,et al.  Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR , 2004, Nature.

[36]  A. Wada,et al.  Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli , 2000, Genes to cells : devoted to molecular & cellular mechanisms.

[37]  R S Balaban,et al.  A new class of contrast agents for MRI based on proton chemical exchange dependent saturation transfer (CEST). , 2000, Journal of magnetic resonance.

[38]  P. Hansen.  Isotope effects on chemical shifts of proteins and peptides , 2000 .

[39]  S. Grzesiek,et al.  NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.

[40]  B. Matthews,et al.  A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene , 1993, Nature.

[41]  Ray Freeman,et al.  Selective excitation in Fourier transform nuclear magnetic resonance. 1978. , 1978, Journal of magnetic resonance.

[42]  H Frauenfelder,et al.  Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.

[43]  A. Redfield,et al.  Double Nuclear Magnetic Resonance Observation of Electron Exchange between Ferri- and Ferrocytochrome c , 1970, Science.

[44]  S. Forsén,et al.  Study of Moderately Rapid Chemical Exchange Reactions by Means of Nuclear Magnetic Double Resonance , 1963 .

[45]  H. Mcconnell.  Reaction Rates by Nuclear Magnetic Resonance , 1958 .

[46]  C D Kroenke,et al.  Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. , 2001, Methods in enzymology.

[47]  Martin Karplus,et al.  Aspects of Protein Reaction Dynamics: Deviations from Simple Behavior , 2000 .

[48]  H. Desvaux,et al.  A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated? , 1999, Journal of magnetic resonance.

[49]  H. Kalbitzer,et al.  Protein NMR Spectroscopy. Principles and Practice , 1997 .