Protein folding while chaperone bound is dependent on weak interactions

Spy is an ATP independent chaperone that allows folding of its client protein Im7 while continuously bound to Spy. Here the authors employ kinetics measurements to study the folding of another Spy client protein SH3 and find that Spy’s ability to allow a client to fold while bound is inversely relat...

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Bibliographic Details
Main Authors: Kevin Wu, Frederick Stull, Changhan Lee, James C. A. Bardwell
Format: article
Language:EN
Published: Nature Portfolio 2019
Subjects:
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Online Access:https://doaj.org/article/8c86c6c179904e2d898f9faec9e90757
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