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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Vydáno v:Journal of the American Chemical Society Ročník 134; číslo 15; s. 6846
Hlavní autoři: 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
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 18.04.2012
Témata:
Disulfides - chemistry
Molecular Dynamics Simulation
Muramidase - chemistry
Protein Conformation
Protein Folding
ISSN:1520-5126, 1520-5126
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Shrnutí: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 bonds. In this comprehensive study, we probe the conformational landscape of non-native states of lysozyme containing a single native disulfide bond utilizing nuclear magnetic resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS), circular dichroism (CD) data, and modeling approaches. The impact on conformational dynamics varies widely depending on the loop size of the single disulfide variants and deviates significantly from random coil predictions for both NMR and SAXS data. From these experiments, we conclude that the introduction of single disulfides spanning a large portion of the polypeptide chain shifts the structure and dynamics of hydrophobic core residues of the protein so that these regions exhibit levels of order comparable to the native state on the nanosecond time scale.
Bibliografie:ObjectType-Article-1
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ISSN:1520-5126
1520-5126
DOI:10.1021/ja3009506