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Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR.

Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Research Abstract Details 

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  • Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Abstract Text:

    s ohkiS Ohki,k miuraK Miura,m saitoM Saito,k nakashimaK Nakashima,h maekawaH Maekawa,m yazawaM Yazawa,s tsudaS Tsuda,k hikichiK Hikichi,

    Using two- and three-dimensional NMR techniques, 1H and main-chain 15N resonances of the N-terminal half domain of yeast calmodulin (YCM0-N) in the presence of Mg2+ and Ca2+ (Mg(2+)-and Ca(2+)-forms) were assigned. The secondary structures of YCM0-N in both forms were determined. The NOESY and 15N-edited NOESY spectra of YCM0-N in each form indicate that there is a hydrophobic core and that two Ca(2+)-binding loops are connected by a short antiparallel beta-sheet. There are four helices (A, B, C, and D named from the N-terminus) for YCM0-N in the Mg(2+)-form. The B-helix is, however, not formed in the Ca(2+)-form. The Ca(2+)-binding of YCM0-N was monitored by (1H,15N)-HSQC at various Ca2+ concentrations. The observed spectral changes as a function of Ca(2+)-concentration can not readily be grouped into a small number of classes; each residue shows individual spectral change. There is no apparent relationship between the spectral change and the type or location of the amino acid concerned.

    Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Publishing Authors By Initials

    s ohkiS Ohki,k miuraK Miura,m saitoM Saito,k nakashimaK Nakashima,h maekawaH Maekawa,m yazawaM Yazawa,s tsudaS Tsuda,k hikichiK Hikichi,

    For similar fungi: ascomycota: saccharomycetales: saccharomyces: saccharomyces cerevisiae research abstracts see: fungi: ascomycota: saccharomycetales: saccharomyces: saccharomyces cerevisiae research

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    Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 119

    Page Numbers: 1045-55

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jun

    YEAR: 1996

    Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Keywords Mesh Terms:

    KEYWORDS: Saccharomyces cerevisiae

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR. Information

    Substance Name: Calcium

    Registry Number: 7440-70-2

    Grant and Affiliation Information for Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR.

    AFFILIATION: High-Resolution NMR Laboratory, Graduate School of Science, Hokkaido University, Sapporo.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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