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


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.

Publication DOI:
Divisions: College of Health & Life Sciences > School of Optometry > Optometry
College of Engineering & Physical Sciences > Systems analytics research institute (SARI)
Uncontrolled Keywords: sugar interactions,biomolecular structures,long molecular dynamics,lysozyme,aqueous trehalose solution,water entrapment hypotheses,Physical and Theoretical Chemistry,Physics and Astronomy(all)
Publication ISSN: 1463-9084
Last Modified: 02 Jan 2024 18:33
Date Deposited: 14 Dec 2011 10:29
Full Text Link: http://pubs.rsc ... 1/CP/c0cp01705a
Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2011-02-14
Authors: Fedorov, Maxim V.
Goodman, Jonathan M.
Nerukh, Dmitry (ORCID Profile 0000-0001-9005-9919)
Schumm, Stephan


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