Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics-Reference-Cited by-同舟云学术

Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics

Published:2000-08-25 Issue:37 Volume:39 Page:11177-11183
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Plaxco Kevin W.¹,Simons Kim T.¹,Ruczinski Ingo¹,Baker David¹

Affiliation:

1. Department of Chemistry and Biochemistry and Interdepartmental Program in Biochemistry and Molecular Biology, University of California, Santa Barbara, Santa Barbara, California 93106, and Departments of Biochemistry and Statistics, University of Washington, Seattle, Washington 98195

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi000200n

Reference66 articles.

1. Pathways for protein folding: is a new view needed?

Cited by 366 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Nonequilibrium relaxation of soft responsive colloids;The Journal of Chemical Physics;2024-09-03

2. Mutational biases favor complexity increases in protein interaction networks after gene duplication;Molecular Systems Biology;2024-03-18

3. Importance of Inter-residue Contacts for Understanding Protein Folding and Unfolding Rates, Remote Homology, and Drug Design;Molecular Biotechnology;2024-03-18

4. Molecular dynamics simulations at high temperatures of the Aeropyrum pernix L7Ae thermostable protein: Insight into the unfolding pathway;Journal of Molecular Graphics and Modelling;2024-03

5. Physics of protein folding;Encyclopedia of Condensed Matter Physics;2024