Probing the Folding Transition State Structure of the Villin Headpiece Subdomain via Side Chain and Backbone Mutagenesis-Reference-Cited by-同舟云学术

Probing the Folding Transition State Structure of the Villin Headpiece Subdomain via Side Chain and Backbone Mutagenesis

Published:2009-05-08 Issue:21 Volume:131 Page:7470-7476
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bunagan Michelle R.¹,Gao Jianmin¹,Kelly Jeffery W.¹,Gai Feng¹

Affiliation:

1. Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, and Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, BCC265, La Jolla, California 92037

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja901860f

Reference66 articles.

1. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain

2. Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets

3. Dominant forces in protein folding

4. In Search of the Energetic Role of Peptide Hydrogen Bonds

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

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