Hyperdimensional protein NMR spectroscopy in peptide-sequence space.

PubWeight™: 1.09‹?› | Rank: Top 10%

🔗 View Article (PMID 17845051)

Published in J Am Chem Soc on September 11, 2007

Authors

Ewen Lescop1, Bernhard Brutscher

Author Affiliations

1: Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1 France.

Articles by these authors

Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc (2005) 2.81

SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR (2005) 2.53

Speeding up three-dimensional protein NMR experiments to a few minutes. J Am Chem Soc (2006) 1.65

A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson (2007) 1.60

Recent advances in solution NMR: fast methods and heteronuclear direct detection. Chemphyschem (2009) 1.34

Direct observation of the dynamic process underlying allosteric signal transmission. J Am Chem Soc (2009) 1.32

BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins. J Biomol NMR (2013) 1.32

Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proc Natl Acad Sci U S A (2007) 1.26

Recovering lost magnetization: polarization enhancement in biomolecular NMR. J Biomol NMR (2010) 1.20

Solution structure of the C-terminal nucleoprotein-RNA binding domain of the vesicular stomatitis virus phosphoprotein. J Mol Biol (2008) 1.10

Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography. J Biol Chem (2006) 1.08

Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: example of longitudinal-relaxation-enhanced BEST-type 1H-15N correlation experiments. J Magn Reson (2009) 1.05

UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. J Am Chem Soc (2007) 1.04

Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr. J Mol Biol (2002) 0.99

Folding of the KIX domain: characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. J Mol Biol (2008) 0.99

Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. J Mol Biol (2012) 0.98

Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. J Am Chem Soc (2009) 0.98

Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-labeled proteins. J Am Chem Soc (2004) 0.97

Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR. J Biol Chem (2009) 0.95

Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains. PLoS One (2013) 0.95

Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex. Nucleic Acids Res (2009) 0.92

HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magn Reson Chem (2006) 0.92

Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. J Am Chem Soc (2009) 0.92

Hadamard amino-acid-type edited NMR experiment for fast protein resonance assignment. J Am Chem Soc (2008) 0.90

NMR spectroscopic studies of intrinsically disordered proteins at near-physiological conditions. Angew Chem Int Ed Engl (2013) 0.89

"CON-CON" assignment strategy for highly flexible intrinsically disordered proteins. J Biomol NMR (2014) 0.88

Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. J Am Chem Soc (2012) 0.86

Highly automated protein backbone resonance assignment within a few hours: the "BATCH" strategy and software package. J Biomol NMR (2009) 0.85

Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load. J Magn Reson (2007) 0.85

Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection. J Am Chem Soc (2003) 0.84

Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. Biochemistry (2005) 0.84

Fast real-time NMR methods for characterizing short-lived molecular states. Chemphyschem (2013) 0.83

13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interactions by NMR spectroscopy: application to the CXCL12α chemokine. J Am Chem Soc (2011) 0.83

Linear phase slope in pulse design: application to coherence transfer. J Magn Reson (2008) 0.83

HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways. J Biomol NMR (2014) 0.82

Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. Biochemistry (2013) 0.82

iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered proteins. J Magn Reson (2011) 0.81

An improved ultrafast 2D NMR experiment: towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. J Biomol NMR (2008) 0.81

Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR. J Magn Reson (2005) 0.81

Optimized set of two-dimensional experiments for fast sequential assignment, secondary structure determination, and backbone fold validation of 13C/15N-labelled proteins. J Biomol NMR (2003) 0.80

1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A. Biomol NMR Assign (2011) 0.79

NMR structure of the cathelin-like domain of the protegrin-3 precursor. Biochemistry (2003) 0.79

Sensitivity-optimized experiment for the measurement of residual dipolar couplings between amide protons. J Biomol NMR (2007) 0.79

Detection and assignment of phosphoserine and phosphothreonine residues by (13)C- (31)P spin-echo difference NMR spectroscopy. J Biomol NMR (2008) 0.79

Biophysical characterization of the MerP-like amino-terminal extension of the mercuric reductase from Ralstonia metallidurans CH34. J Biol Inorg Chem (2003) 0.79

Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain. Biochemistry (2002) 0.79

Direct structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution. J Am Chem Soc (2002) 0.78

Suppression of artifacts induced by homonuclear decoupling in amino-acid-type edited methyl 1H-13C correlation experiments. J Magn Reson (2004) 0.78

Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. J Am Chem Soc (2007) 0.78

Measuring hydrogen exchange in proteins by selective water saturation in (1)H- (15)N SOFAST/BEST-type experiments: advantages and limitations. J Biomol NMR (2014) 0.77

Probing conformational exchange dynamics in a short-lived protein folding intermediate by real-time relaxation-dispersion NMR. J Am Chem Soc (2017) 0.77

Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins. J Biomol NMR (2011) 0.77

Selective isotopic unlabeling of proteins using metabolic precursors: application to NMR assignment of intrinsically disordered proteins. Chembiochem (2012) 0.76

Side chain orientation from methyl 1H-1H residual dipolar couplings measured in highly deuterated proteins. J Am Chem Soc (2002) 0.75

Parallel screening and optimization of protein constructs for structural studies. Protein Sci (2009) 0.75

Resolution-enhanced base-type-edited HCN experiment for RNA. J Biomol NMR (2005) 0.75

NMR study of the interaction between Zn(II) ligated bleomycin and Streptoalloteichus hindustanus bleomycin resistance protein. Biochemistry (2003) 0.75