Deuteration effects on the conformational dynamics of proteins in a trehalose glass

J. Schlichter, J. Friedrich, L. Herenyi, J. Fidy

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4 Citations (Scopus)


We present results of a hole-burning spectral diffusion experiment On a deuterated sample of horseradish peroxidase (substituted with free-base mesoporphyrin-IX) in a trehalose/glycerol glass. Like in earlier experiments, the spectral diffusion dynamics is well-described by a diffusion picture; the most noticeable observation is a power-law dependence of the hole-broadening on time. In addition, the comparison of the present data with our earlier experiments allows for a microscopic interpretation of the influence of trehalose on protein dynamics. Here, internal water molecules in the proteins seem to be of great importance.

Original languageEnglish
Pages (from-to)3510-3514
Number of pages5
JournalJournal of Physical Chemistry B
Issue number13
Publication statusPublished - Apr 4 2002


ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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