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Scanning Electron Microscopic Analysis of Glycated Histone H2B

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  • Abdul Rouf Mir

    (Department of Biotechnology, University of Kashmir Jammu and Kashmir, India)

Abstract

Glycation is a widely reported modification of proteins. It leads to the compromise in the structural integrity of the proteins and have been widely implicated in pathological problems. While a large number of protein structures have been analysed for post glycation effects, no work reports changes in histone H2B upon non enzymatic glycation. The work presents the scanning electron micrographic study on the structure of histone H2B derived from calf thymus after its modification by an oxo-aldehyde named methylgyoxal. The results reveal a complete different look of H2B post modification under SEM, and the images point towards the amorphous aggregate adduct generation. While, many protein modifications may have little significance, the modifications of H2B can have severe impact on the gene expression and epigenetics as it is a part of core histone octamer. The work needs to be taken forward for further analysis.

Suggested Citation

  • Abdul Rouf Mir, 2017. "Scanning Electron Microscopic Analysis of Glycated Histone H2B," Current Trends in Biomedical Engineering & Biosciences, Juniper Publishers Inc., vol. 4(2), pages 12-14, May.
    • Handle: RePEc:adp:jctbeb:v:4:y:2017:i:2:p:12-14
    DOI: 10.19080/CTBEB.2017.04.555631
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    References listed on IDEAS

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    1. Monica Bucciantini & Elisa Giannoni & Fabrizio Chiti & Fabiana Baroni & Lucia Formigli & Jesús Zurdo & Niccolò Taddei & Giampietro Ramponi & Christopher M. Dobson & Massimo Stefani, 2002. "Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases," Nature, Nature, vol. 416(6880), pages 507-511, April.
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