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15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions.

15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Research Abstract Details 

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  • 15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Abstract Text:

    xuanjun aiXuanjun Ai,zheng zhouZheng Zhou,yawen baiYawen Bai,wing-yiu choyWing-Yiu Choy,

    The effects of macromolecular crowding on protein stability and folding kinetics have been studied using the recently developed 15N spin relaxation dispersion technique. By applying this method to a redesigned apocytochrome b562, the kinetics and thermodynamics of the protein folding processes in both the presence and the absence of crowding agents have been characterized. The result indicates that, even under the mild crowded environments (in the presence of 85 mg/mL of PEG 20K), the folding rate of the protein can speed up significantly while the unfolded rate remains unchanged within experimental error.

    15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Publishing Authors By Initials

    x aiX Ai,z zhouZ Zhou,y baiY Bai,wy choyWY Choy,

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

    PUBMED ID PMID:

    MEDLINE DATE:

    15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of the American Chemical Society

    VOLUME: 128

    Page Numbers: 3916-7

    Journal Abbreviation: J. Am. Chem. Soc.

    ISSN: 0002-7863

    DAY: 29

    MONTH: Mar

    YEAR: 2006

    15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7503056

    15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Keywords Mesh Terms:

    KEYWORDS: Thermodynamics

    MESH TERMS: methods

    Chemical & Substance for Abstract: 15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions. Information

    Substance Name: Nitrogen Isotopes

    Registry Number: 0

    Grant and Affiliation Information for 15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions.

    AFFILIATION: Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Am Chem Soc

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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