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    Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation

    Yoneda, J.S. and Miles, Andrew J. and Araujo, A.P.U. and Wallace, Bonnie A. (2017) Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Science 26 (4), pp. 718-726. ISSN 0961-8368.

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    Abstract

    Globular proteins composed of different secondary structures and fold types were examined by synchrotron radiation circular dichroism spectroscopy to determine the effects of dehydration on their secondary structures. They exhibited only minor changes upon removal of bulk water during film formation, contrary to previously reported studies of proteins dehydrated by lyophilization (where substantial loss of helical structure and gain in sheet structure was detected). This near lack of conformational change observed for globular proteins contrasts with intrinsically disordered proteins (IDPs) dried in the same manner: the IDPs, which have almost completely unordered structures in solution, exhibited increased amounts of regular (mostly helical) secondary structures when dehydrated, suggesting formation of new intra-protein hydrogen bonds replacing solvent-protein hydrogen bonds, in a process which may mimic interactions that occur when IDPs bind to partner molecules. This study has thus shown that the secondary structures of globular and intrinsically disordered proteins behave very differently upon dehydration, and that films are a potentially useful format for examining dehydrated soluble proteins and assessing IDPs structures.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): globular proteins, intrinsically disordered proteins, synchrotron radiation circular dichroism (SRCD) spectroscopy, dehydration, unfolding, folding, secondary structure
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 15 Feb 2017 12:40
    Last Modified: 26 Jul 2019 19:35
    URI: http://eprints.bbk.ac.uk/id/eprint/18167

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