Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution
Top Cited Papers
- 26 April 2006
- journal article
- review article
- Published by American Chemical Society (ACS) in Chemical Reviews
- Vol. 106 (5) , 1672-1699
- https://doi.org/10.1021/cr040422h
Abstract
No abstract availableThis publication has 135 references indexed in Scilit:
- Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional ConsequencesChemical Reviews, 2006
- Evolutionarily conserved networks of residues mediate allosteric communication in proteinsNature Structural & Molecular Biology, 2002
- Side-chain Dynamics of the SAP SH2 Domain Correlate with a Binding Hot Spot and a Region with Conformational PlasticityJournal of Molecular Biology, 2002
- Protein NMR relaxation: theory, applications and outlookProgress in Nuclear Magnetic Resonance Spectroscopy, 1998
- Energetics of target peptide recognition by calmodulin: A calorimetric studyJournal of Molecular Biology, 1997
- Selective Methyl Group Protonation of Perdeuterated ProteinsJournal of Molecular Biology, 1996
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic TumblingScience, 1995
- Backbone Dynamics of Ribonuclease HI: Correlations with Structure and Function in an Active EnzymeJournal of Molecular Biology, 1995
- Carbon-13 nuclear magnetic resonance relaxation-derived .psi., .PHI. bond rotational energy barriers and rotational restrictions for glycine 13C.alpha.-methylenes in a GXX-repeat hexadecapeptideBiochemistry, 1993