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Mapping polypeptide self-recognition through (1)H off-resonance relaxation.

Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Research Abstract Details 

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  • Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Abstract Text:

    veronica espositoVeronica Esposito,rahul dasRahul Das,giuseppe melaciniGiuseppe Melacini,

    1H NMR relaxation rates provide a readily available and sensitive probe ideally suited to investigate the weak (KD approximately micromolar to millimolar range) interactions that frequently mediate polypeptide oligomerization in the early steps of amyloid fibrillogenesis. However, the measurement of transverse and longitudinal 1H relaxation rates is experimentally challenging due to J-transfer and selectivity problems in CPMG and inversion-recovery experiments, respectively. We show here that these problems are effectively circumvented by measuring nonselective off-resonance relaxation rates using an effective field tilted by 35.5 degrees . When applied to the Halpha spins of the Abeta (12-28) peptide, the proposed experiment provides a residue-resolution self-recognition map which is fully consistent with previous independent mutational studies. The method is anticipated to be widely applicable not only to the fast growing family of amyloidogenic peptides but also to the screening and mapping of protein-ligand interactions in general.

    Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Publishing Authors By Initials

    v espositoV Esposito,r dasR Das,g melaciniG Melacini,

    For similar peptides research abstracts see: peptides research

    PUBMED ID PMID:

    MEDLINE DATE:

    Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Journal Published:

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

    Journal: Journal of the American Chemical Society

    VOLUME: 127

    Page Numbers: 9358-9

    Journal Abbreviation: J. Am. Chem. Soc.

    ISSN: 0002-7863

    DAY: 6

    MONTH: Jul

    YEAR: 2005

    Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7503056

    Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Keywords Mesh Terms:

    KEYWORDS: Peptides

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Mapping polypeptide self-recognition through (1)H off-resonance relaxation. Information

    Substance Name: Hydrogen

    Registry Number: 1333-74-0

    Grant and Affiliation Information for Mapping polypeptide self-recognition through (1)H off-resonance relaxation.

    AFFILIATION: Departments of Chemistry, Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street W., Hamilton, Ontario L8S 4M1, Canada.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Am Chem Soc

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