Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism-Reference-Cited by-同舟云学术

Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism

Published:2000-02-15 Issue:4 Volume:97 Page:1525-1529
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Fersht A. R.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference29 articles.

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

2. Mapping the transition state and pathway of protein folding by protein engineering

3. Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships

4. Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships

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