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Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Research Abstract Details 

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  • Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Abstract Text:

    minghui wangMinghui Wang,yuefeng tangYuefeng Tang,satoshi satoSatoshi Sato,liliya vugmeysterLiliya Vugmeyster,c james mcknightC James McKnight,daniel p raleighDaniel P Raleigh,

    There is considerable interest in small proteins that fold very rapidly. These proteins have become attractive targets for both theoretical and computational studies. The independently folded 36-residue villin headpiece subdomain has been the subject of a number of such studies and is predicted to fold quickly. We demonstrate using dynamic NMR line-shape analysis that the protein folds on the time scale of 10 mus. Folding rates were directly estimated between 56 and 78 degrees C using resolved protein resonances from three different residues at both 500 and 700 MHz. The rates estimated using different residues and different field strengths agree well with each other. The estimated folding rate lies between 0.5 and 2.0 x 105 s-1 over this temperature range. The folding rate depends only weakly on temperature.

    Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Publishing Authors By Initials

    m wangM Wang,y tangY Tang,s satoS Sato,l vugmeysterL Vugmeyster,cj mcknightCJ McKnight,dp raleighDP Raleigh,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein folding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein folding research

    PUBMED ID PMID:

    MEDLINE DATE:

    Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Journal of the American Chemical Society

    VOLUME: 125

    Page Numbers: 6032-3

    Journal Abbreviation: J. Am. Chem. Soc.

    ISSN: 0002-7863

    DAY: 21

    MONTH: May

    YEAR: 2003

    Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7503056

    Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Keywords Mesh Terms:

    KEYWORDS: Protein Folding

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Information

    Substance Name: villin headpiece subdomain peptide

    Registry Number: 0

    Grant and Affiliation Information for Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

    AFFILIATION: Department of Chemistry, State University of New York at Stony Brook, 11794-3400, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM 62886

    ACRONYM: GM

    MEDLINETA: J Am Chem Soc

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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