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Protein dynamics at low temperatures

  • Technical University of Munich
  • Semmelweis University

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

The low temperature conformational dynamics of the heme type protein mesoporphyrin-IX-substituted horseradish peroxidase is investigated by spectral diffusion waiting time/ aging experiments. Spectral diffusion broadening is governed by a power law in time. There is a small but significant aging effect. It is assumed that the conformational dynamics of the protein which leads to the spectral broadening of the burnt-in holes is governed by a diffusion type equation. In this case the shape of the spectral diffusion kernel is Gaussian. This model is contrasted with spectral diffusion phenomena as described by the TLS-model (TLS, two level system).

Original languageEnglish
Pages (from-to)3045-3050
Number of pages6
JournalJournal of Chemical Physics
Volume112
Issue number6
DOIs
StatePublished - 8 Feb 2000

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