Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding-Reference-Cited by-同舟云学术

Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding

Published:1998-09-25 Issue:41 Volume:37 Page:14613-14622
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kentsis Alex¹,Sosnick Tobin R.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, Illinois 60637

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi981641y

Reference53 articles.

1. Native-like β-structure in a Trifluoroethanol-induced Partially Folded State of the All-β-sheet Protein Tendamistat

2. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure

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