Hydrogen exchange and structural dynamics of proteins and nucleic acids

SW Englander, NR Kallenbach - Quarterly reviews of biophysics, 1983 - cambridge.org
Though the structures presented in crystallographic models of macromolecules appear to
possess rock-like solidity, real proteins and nucleic acids are not particularly rigid. Most …

Protein folding.

TE Creighton - Biochemical journal, 1990 - ncbi.nlm.nih.gov
1. THE PROTEIN FOLDING PROBLEM To be biologically active, all proteins must adopt
specific folded three-dimensional structures. Yet the genetic information for the protein …

Paramagnetic metal complexes as water proton relaxation agents for NMR imaging: theory and design

RB Lauffer - Chemical reviews, 1987 - ACS Publications
The development of nuclear magnetic resonance (NMR) imaging techniques as a clinical
diagnostic modality has prompted the need for a new class of pharmaceuticals. These drugs …

Quasielastic neutron scattering

M Bée - 1988 - inis.iaea.org
[en] This book provides an in-depth study of quasielastic neutron scattering both for
specialists in this subject and for those who work in related fields such as NMR, infrared and …

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

KA Henzler-Wildman, M Lei, V Thai, SJ Kerns… - Nature, 2007 - nature.com
The synergy between structure and dynamics is essential to the function of biological
macromolecules. Thermally driven dynamics on different timescales have been …

Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins

GM Clore, A Szabo, A Bax, LE Kay… - Journal of the …, 1990 - ACS Publications
Deviations from the simple two-parameter model-free approach to the interpretation of
nitrogen-15 nuclear magnetic relaxation of Page 1 J. Am. Chem. Soc. 1990, 112, 4989-4991 …

Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.

B Brooks, M Karplus - … of the National Academy of Sciences, 1983 - National Acad Sciences
A normal mode analysis making use of an empirical potential function including local and
nonlocal (nonbonded) interactions is performed for the bovine pancreatic trypsin inhibitor in …

Intrinsic motions along an enzymatic reaction trajectory

KA Henzler-Wildman, V Thai, M Lei, M Ott, M Wolf-Watz… - Nature, 2007 - nature.com
The mechanisms by which enzymes achieve extraordinary rate acceleration and specificity
have long been of key interest in biochemistry. It is generally recognized that substrate …

[BOOK][B] Proteins: A Theoretical Perspective of Dynamics, Structure, and Thermodynamics, Volume 71

I Prigogine, SA Rice - 2009 - books.google.com
Presenting a wide-ranging view of current developments in protein research, the papers in
this collection, each written by highly regarded experts in the field, examine various aspects …

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme

M Levitt, C Sander, PS Stern - Journal of molecular biology, 1985 - Elsevier
We have developed a new method for modelling protein dynamics using normal-mode
analysis in internal co-ordinates. This method, normal-mode dynamics, is particularly well …