Stability and Folding Kinetics of a Ubiquitin Mutant with a Strong Propensity for Nonnative β-Hairpin Conformation in the Unfolded State-Reference-Cited by-同舟云学术

Stability and Folding Kinetics of a Ubiquitin Mutant with a Strong Propensity for Nonnative β-Hairpin Conformation in the Unfolded State

Published:2003-10-25 Issue:46 Volume:42 Page:13762-13771
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Platt Geoffrey W.¹,Simpson Stephen A.¹,Layfield Robert¹,Searle Mark S.¹

Affiliation:

1. School of Chemistry, University Park, Nottingham, NG7 2RD, United Kingdom, and School of Biomedical Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi030147d

Reference57 articles.

1. Protein folding mechanisms: new methods and emerging ideas

2. Protein folding: from the levinthal paradox to structure prediction

3. Jackson, S. E. How do small single domain proteins fold? (1998)Folding Des. 3, R81−R91.

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