Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins: Extent of Protein Unfolding

C. Nick Pace; Beatrice M. P. Huyghues-Despointes; Hailong Fu; Kazufumi Takano; J. Martin Scholtz; Gerald R. Grimsley

doi:10.1002/pro.370

Back

Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins: Extent of Protein Unfolding

Journal article

Open access

Peer reviewed

Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins: Extent of Protein Unfolding

C. Nick Pace, Beatrice M. P. Huyghues-Despointes, Hailong Fu, Kazufumi Takano, J. Martin Scholtz and Gerald R. Grimsley

Protein science, Vol.19(5), pp.929-943

05/2010

DOI: 10.1002/pro.370

PMCID: PMC2868236

PMID: 20198681

Files and links (1)

url

https://doi.org/10.1002/pro.370View

Published (Version of record) Open Access

Abstract

The goal of this article is to gain a better understanding of the denatured state ensemble (DSE) of proteins through an experimental and computational study of their denaturation by urea. Proteins unfold to different extents in urea and the most hydrophobic proteins have the most compact DSE and contain almost as much secondary structure as folded proteins. Proteins that unfold to the greatest extent near pH 7 still contain substantial amounts of secondary structure. At low pH, the DSE expands due to charge-charge interactions and when the net charge per residue is high, most of the secondary structure is disrupted. The proteins in the DSE appear to contain substantial amounts of polyproline II conformation at high urea concentrations. In all cases considered, including staph nuclease, the extent of unfolding by urea can be accounted for using the data and approach developed in the laboratory of Wayne Bolen (Auton et al., Proc Natl Acad Sci 2007; 104:15317-15323).

Details

Title: Subtitle: Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins: Extent of Protein Unfolding
Creators: C. Nick Pace
Beatrice M. P. Huyghues-Despointes - Texas A&M Health Science Center
Hailong Fu - Texas A&M University
Kazufumi Takano - Osaka University
J. Martin Scholtz - Texas A&M University
Gerald R. Grimsley - Texas A&M Health Science Center
Resource Type: Journal article
Publication Details: Protein science, Vol.19(5), pp.929-943
DOI: 10.1002/pro.370
PMID: 20198681
PMCID: PMC2868236
ISSN: 0961-8368
eISSN: 1469-896X
Grant note: name: NIH, award: GM 37039, GM 52483; DOI: 10.13039/100000928, name: Robert A. Welch Foundation, award: BE-1060, BE-1281; name: Tom and Jean McMullin Professorship
Language: English
Date published: 05/2010
Academic Unit: Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
Record Identifier: 9984288732502771

Metrics

33 Record Views

38 Times Cited - Web of Science