Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy

Yutaka Shibata, Atusi Kurita, Takashi Kushida

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Equilibrium fluctuations of the protein conformation have been studied in myoglobin by a novel method of time-resolved transient hole-burning spectroscopy over a temperature range of 180-300 K and a time range of 10 ns to 10 ms. The temporal shift of the hole spectrum has been observed in a wide temperature region of 200-300 K. It has been found that the time behavior of the peak position of the hole is highly nonexponential and can be expressed by a stretched exponential function with a β value of 0.22. As compared with the results for a dye solution sample, the time scale of the fluctuation of the protein conformation is much more weakly dependent on temperature. The time scale of the observed conformational dynamics shows a temperature dependence similar to that associated with the ligand escape process of myoglobin.

Original languageEnglish
Pages (from-to)521-527
Number of pages7
JournalBiophysical Journal
Volume75
Issue number1
DOIs
Publication statusPublished - 1998 Jul

ASJC Scopus subject areas

  • Biophysics

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