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Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR.

Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Research Abstract Details 

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  • Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Abstract Text:

    masafumi d yamadaMasafumi D Yamada,shinsaku marutaShinsaku Maruta,satoshi yasudaSatoshi Yasuda,kazunori kondoKazunori Kondo,hidekatsu maedaHidekatsu Maeda,toshiaki arataToshiaki Arata,masafumi d yamadaMasafumi D Yamada,shinsaku marutaShinsaku Maruta,satoshi yasudaSatoshi Yasuda,kazunori kondoKazunori Kondo,hidekatsu maedaHidekatsu Maeda,toshiaki arataToshiaki Arata,

    The EPR spectra of the spin labels attached to loops L11 and L12 of kinesin were resolved into slow (rotational correlation time, tau=10-45 ns) and fast (tau=2 ns) components. The fraction of the slow component increased considerably when kinesin was complexed with a microtubule (MT). On MT binding and in the presence of nucleotides ADP and AMPPNP, the spin labels on L11, particularly at A252C and L249C, significantly decreased the fraction of the slow component. Moreover, dipolar EPR detected a wide distribution in distance range, 1-2 nm between the two spin labels attached to T242C/A252C or A247C/A252C; this distribution was slightly narrower in the presence of MTs than in their absence. These results suggested that the L11 residues undergo conformational transition on the binding of nucleotides and MT, while these residues remained to fluctuate over a nanometer range.

    Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Publishing Authors By Initials

    md yamadaMD Yamada,s marutaS Maruta,s yasudaS Yasuda,k kondoK Kondo,h maedaH Maeda,t arataT Arata,md yamadaMD Yamada,s marutaS Maruta,s yasudaS Yasuda,k kondoK Kondo,h maedaH Maeda,t arataT Arata,

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    Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Journal Published:

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

    Journal: Biochemical and biophysical research communication

    VOLUME: 364

    Page Numbers: 620-6

    Journal Abbreviation: Biochem. Biophys. Res. Commun.

    ISSN: 1090-2104

    DAY: 16

    MONTH: 10

    YEAR: 2007

    Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Information

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    LANGUAGE: eng

    NlmUniqueID: 372516

    Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR. Keywords Mesh Terms:

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    Grant and Affiliation Information for Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR.

    AFFILIATION: Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Biochem Biophys Res Commun

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