Effects of altered backbone composition on the folding kinetics and mechanism of an ultrafast-folding protein

Author:

Santhouse Jacqueline R.1,Leung Jeremy M. G.1ORCID,Chong Lillian T.1ORCID,Horne W. Seth1ORCID

Affiliation:

1. Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA

Abstract

Analysis of folding rates and folding mechanism in tertiary structure mimetics reveals pronounced context-dependent effects of artificial backbone connectivity on the folding process.

Funder

National Science Foundation

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Reference54 articles.

1. Richard Feynman’s blackboard at the time of his death, 1988, 1.10-67, Caltech Photographs, California Institute of Technology Archives and Special Collections, https://collections.archives.caltech.edu/repositories/2/archival_objects/106392 , accessed June 9, 2023

2. Foldamers:  A Manifesto

3. A Field Guide to Foldamers

4. Sophistication of foldamer form and function in vitro and in vivo

5. Foldamers as versatile frameworks for the design and evolution of function

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