Early Turn Formation and Chain Collapse Drive Fast Folding of the Major Cold Shock Protein CspA of Escherichia coli-Reference-Cited by-同舟云学术

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Early Turn Formation and Chain Collapse Drive Fast Folding of the Major Cold Shock Protein CspA of Escherichia coli

Published:2012-11-01 Issue:45 Volume:51 Page:9104-9111
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Vu Dung M.¹,Brewer Scott H.²,Dyer R. Brian³

Affiliation:

1. Chemistry Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, United States

2. Department of Chemistry, Franklin & Marshall College, Lancaster, Pennsylvania 17604, United States

3. Department of Chemistry, Emory University, Atlanta, Georgia 30322, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301296y

Reference58 articles.

1. Critical nucleation size in the folding of small apparently two-state proteins

2. How do small single-domain proteins fold?

3. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

4. Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright

5. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein

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