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

Maxim V. Fedorov, Jonathan M. Goodman, Dmitry Nerukh, Stephan Schumm

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)2294-2299
Number of pages6
JournalPhysical Chemistry Chemical Physics
Issue number6
Publication statusPublished - 14 Feb 2011


  • sugar interactions
  • biomolecular structures
  • long molecular dynamics
  • lysozyme
  • aqueous trehalose solution
  • water entrapment hypotheses


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