NMR Characterization of a Peptide Model Provides Evidence for Significant Structure in the Unfolded State of the Villin Headpiece Helical Subdomain-Reference-Cited by-同舟云学术

NMR Characterization of a Peptide Model Provides Evidence for Significant Structure in the Unfolded State of the Villin Headpiece Helical Subdomain

Published:2006-05-13 Issue:22 Volume:45 Page:6940-6946
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tang Yuefeng¹,Goger Michael J.¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry, State University of New York, Stony Brook, New York 11790-3400, New York Structural Biology Center, 89 Convent Avenue, New York, New York 10027-7556, and Graduate Program in Biochemistry and Structure Biology, State University of New York, Stony Brook, New York 11794

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi052484n

Reference49 articles.

1. Favourable native-like helical local interactions can accelerate protein folding

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

3. Early events in protein folding

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