Modulation of structure and dynamics by disulfide bond formation in unfolded states

During oxidative folding, the formation of disulfide bonds has profound effects on guiding the protein folding pathway. Until now, comparatively little is known about the changes in the conformational dynamics in folding intermediates of proteins that contain only a subset of their native disulfide...

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Bibliographic Details

Published in:	Journal of the American Chemical Society Vol. 134; no. 15; p. 6846
Main Authors:	Silvers, Robert, Sziegat, Friederike, Tachibana, Hideki, Segawa, Shin-ichi, Whittaker, Sara, Günther, Ulrich L, Gabel, Frank, Huang, Jie-rong, Blackledge, Martin, Wirmer-Bartoschek, Julia, Schwalbe, Harald
Format:	Journal Article
Language:	English
Published:	United States 18.04.2012
Subjects:	Disulfides - chemistry Molecular Dynamics Simulation Muramidase - chemistry Protein Conformation Protein Folding
ISSN:	1520-5126, 1520-5126
Online Access:	Get more information
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