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Physical methods used to study core histone tail structures and interactions in solution.

Physical methods used to study core histone tail structures and interactions in solution. Research Abstract Details 

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  • Physical methods used to study core histone tail structures and interactions in solution. Abstract Text:

    xiaodong wangXiaodong Wang,jeffrey j hayesJeffrey J Hayes,

    The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structures and binding behavior of the tail domains in various chromatin environments. All of these methods indicate that the tail domains bind primarily electrostatically to sites within chromatin. The data also indicate that the tails adopt specific structures when bound to DNA and that tail structures and interactions are plastic, depending on the specific chromatin environment. In addition, post-translational modifications, such as acetylation, can directly alter histone tail structures and interactions.

    Physical methods used to study core histone tail structures and interactions in solution. Publishing Authors By Initials

    x wangX Wang,jj hayesJJ Hayes,

    For similar abstracts research abstracts see: abstracts research

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    Physical methods used to study core histone tail structures and interactions in solution. Journal Published:

    PUBLICATION TYPE: Review

    Journal: Biochemistry and cell biology = Biochimie et biolo

    VOLUME: 84

    Page Numbers: 578-88

    Journal Abbreviation:

    ISSN: 0829-8211

    DAY: 3

    MONTH: Aug

    YEAR: 2006

    Physical methods used to study core histone tail structures and interactions in solution. Information

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    LANGUAGE: eng

    NlmUniqueID: 8606068

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    Grant and Affiliation Information for Physical methods used to study core histone tail structures and interactions in solution.

    AFFILIATION: Department of Biochemistry and Biophysics, Box 712, University of Rochester Medical Center, 601 Elmwood Avenue, Rochester NY, USA.

    Country: Canada

    Canada Research PublicationCanada Research Publication

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    MEDLINETA: Biochem Cell Biol

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