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Issue 6, 2011
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Self-assembly of trehalose molecules on a lysozyme surface: the broken glass hypothesis

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Abstract

To help understand how sugar interactions with proteins stabilise biomolecular structures, we compare the three main hypotheses for the phenomenon with the results of long molecular dynamics simulations on lysozyme in aqueous trehalose solution (0.75 M). We show that the water replacement and water entrapment hypotheses need not be mutually exclusive, because the trehalose molecules assemble in distinctive clusters on the surface of the protein. The flexibility of the protein backbone is reduced under the sugar patches supporting earlier findings that link reduced flexibility of the protein with its higher stability. The results explain the apparent contradiction between different experimental and theoretical results for trehalose effects on proteins.

Graphical abstract: Self-assembly of trehalose molecules on a lysozyme surface: the broken glass hypothesis

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Publication details

The article was received on 03 Sep 2010, accepted on 26 Oct 2010 and first published on 29 Nov 2010


Article type: Paper
DOI: 10.1039/C0CP01705A
Citation: Phys. Chem. Chem. Phys., 2011,13, 2294-2299
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    Self-assembly of trehalose molecules on a lysozyme surface: the broken glass hypothesis

    M. V. Fedorov, J. M. Goodman, D. Nerukh and S. Schumm, Phys. Chem. Chem. Phys., 2011, 13, 2294
    DOI: 10.1039/C0CP01705A

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