Denatured state effects and the origin of nonclassical phi values in protein folding.

Denatured state effects and the origin of nonclassical phi values in protein folding. Research Abstract Details 

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Denatured state effects and the origin of nonclassical phi values in protein folding. Abstract Text:

Jae-Hyun Cho,Daniel P Raleigh,Jae-Hyun Cho,Daniel P Raleigh,

Denatured state effects and the origin of nonclassical phi values in protein folding. Publishing Authors By Initials

JH Cho,DP Raleigh,JH Cho,DP Raleigh,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

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Denatured state effects and the origin of nonclassical phi values in protein folding. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of the American Chemical Society

VOLUME: 128

Page Numbers: 16492-3

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 27

MONTH: Dec

YEAR: 2006

Denatured state effects and the origin of nonclassical phi values in protein folding. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

Denatured state effects and the origin of nonclassical phi values in protein folding. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: chemistry

Chemical & Substance for Abstract: Denatured state effects and the origin of nonclassical phi values in protein folding. Information

Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Denatured state effects and the origin of nonclassical phi values in protein folding.

AFFILIATION: Graduate Program in Biochemistry and Structural Biology, Department of Chemistry, State University of New York at Stony Brook, Stony Brook, NY 11794-3400, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 70941

ACRONYM: GM

MEDLINETA: J Am Chem Soc

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