Visualizing transient dark states by NMR spectroscopy

NJ Anthis, GM Clore - Quarterly Reviews of Biophysics, 2015 - cambridge.org
Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

Heme protein assemblies

CJ Reedy, BR Gibney - Chemical reviews, 2004 - ACS Publications
Hemes remain one of the most visible and versatile classes of cofactors utilized in biology. 1
Since their discovery, the structural and functional aspects of heme proteins have fascinated …

Protein folding intermediates and pathways studied by hydrogen exchange

SW Englander - Annual review of biophysics and biomolecular …, 2000 - annualreviews.org
▪ Abstract In order to solve the immensely difficult protein-folding problem, it will be
necessary to characterize the barriers that slow folding and the intermediate structures that …

Protein folding: the stepwise assembly of foldon units

H Maity, M Maity, MMG Krishna… - Proceedings of the …, 2005 - National Acad Sciences
Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is
composed of five foldon units that continually unfold and refold even under native …

Protein dynamics viewed by hydrogen exchange

JJ Skinner, WK Lim, S Bédard, BE Black… - Protein …, 2012 - Wiley Online Library
To examine the relationship between protein structural dynamics and measurable hydrogen
exchange (HX) data, the detailed exchange behavior of most of the backbone amide …

Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry

W Hu, BT Walters, ZY Kan, L Mayne… - Proceedings of the …, 2013 - National Acad Sciences
The kinetic folding of ribonuclease H was studied by hydrogen exchange (HX) pulse
labeling with analysis by an advanced fragment separation mass spectrometry technology …

Protein folding and misfolding: mechanism and principles

SW Englander, L Mayne, MMG Krishna - Quarterly reviews of …, 2007 - cambridge.org
Two fundamentally different views of how proteins fold are now being debated. Do proteins
fold through multiple unpredictable routes directed only by the energetically downhill nature …

Chaperonin function: folding by forced unfolding

M Shtilerman, GH Lorimer, S Walter Englander - Science, 1999 - science.org
The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was
detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate …

A statistical thermodynamic model of the protein ensemble

VJ Hilser, B García-Moreno E, TG Oas, G Kapp… - Chemical …, 2006 - ACS Publications
To understand the structural basis of biology, it is necessary to understand the
transformations of macromolecules during functional cycles. These changes can involve …

Hydrogen exchange in peptides and proteins using NMR spectroscopy

CE Dempsey - Progress in Nuclear Magnetic Resonance …, 2001 - Elsevier
Analysis of the kinetics of hydrogen exchange in biological macromolecules is a powerful
method for studying both their structural and dynamic properties. This arises from our …