Fluctuations of conformational states in biological molecules: Theory for anomalous spectral diffusion dynamics

A. L. Burin*, Yu A. Berlin, A. Z. Patashinski, M. A. Ratner, J. Friedrich

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

An anomalous power law behavior of spectral diffusion broadening of persistent holes is found in large biological molecules dissolved in a glassy host at very low temperature. We argue that this is caused by the internal degrees of freedom of the biomolecule itself rather than by excitations of the glassy host. To explain the observed universal time dependence of the hole width w ∼ t1/4, we propose a stochastic model of protein dynamics close to the equilibrium, which describes this process in terms of the quasi-one-dimensional diffusion of proteins in conformation space. Assuming that each step of diffusive motion changes the electronic excitation energy randomly, we derive the observed time behavior of the spectral hole. The physical mechanisms involved are discussed.

Original languageEnglish (US)
Pages (from-to)321-323
Number of pages3
JournalPhysica B: Condensed Matter
Volume316-317
DOIs
StatePublished - May 2002

Funding

This work is supported by MRSEC/NSF program (Grant No. DMR-0076097), by the Chemistry Division of the NSF and ONR, and by the DOD/MURI program. One of us (J.F.) are grateful to DFG (SFB 533, B5) and the Fonds der Chemischen Industrie for financial support. We also acknowledge organizers and participants of the International Workshop on “Collective Phenomena in the Low Temperature Physics of Glasses” (Dresden, 2000) for useful discussions.

Keywords

  • Hole burning
  • Proteins
  • Spectral diffusion
  • Strain interaction

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Electrical and Electronic Engineering

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