Temperature and solvent viscosity dependence of conformational dynamics of Zn-substituted myoglobin observed by nanosecond time-resolved transient hole-burning spectroscopy

Y. Shibata, H. Takahashi, A. Kurita, T. Kushida

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Conformational fluctuations of a protein myoglobin in solution have been investigated by a time-resolved transient hole-burning experiment with a temporal resolution of ≃10 ns over the temperature range of 180-300 K. The temperature dependence of the observed relaxation time τr has been well fitted by the Vogel-Fulcher law. The solvent viscosity dependence of τr has been also studied around room temperature.

Original languageEnglish
Pages (from-to)605-606
Number of pages2
JournalJournal of Luminescence
Volume72-74
DOIs
Publication statusPublished - 1997 Jun
Externally publishedYes

Keywords

  • Conformational relaxation
  • Myoglobin
  • Solvent viscosity
  • Transient hole-burning

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Chemistry(all)
  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics

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