Spectrally and time-resolved fluorescence spectroscopic study on melittin-calmodulin interaction

Takuhiro Otosu, Etsuko Nishimoto, Shoji Yamashita

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The origin of multi-exponential fluorescence decay property of tryptophan (Trp) in protein has been in controversy, and dielectric relaxation is thought to be one of the most plausible candidates of that origin. In this study, we studied melittin-calmodulin interaction on the concept of dielectric relaxation by spectrally and time-resolved fluorescence spectroscopy. Trp residue in melittin demonstrated drastic change in its dielectric relaxation rate and scale by binding with calmodulin. Expected change of relaxation rate suggested that dielectric relaxation accounts for multi-exponential property of fluorescence decay. We also examined the time variation of radiative and non-radiative decay rates. That result demonstrated the distinct difference profiles of non-radiative decay rate of Trp in melittin and the complex.

Original languageEnglish
Pages (from-to)655-661
Number of pages7
JournalJournal of biochemistry
Volume142
Issue number5
DOIs
Publication statusPublished - Nov 1 2007

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Melitten
Dielectric relaxation
Calmodulin
Tryptophan
Fluorescence
Fluorescence Spectrometry
Fluorescence spectroscopy
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Spectrally and time-resolved fluorescence spectroscopic study on melittin-calmodulin interaction. / Otosu, Takuhiro; Nishimoto, Etsuko; Yamashita, Shoji.

In: Journal of biochemistry, Vol. 142, No. 5, 01.11.2007, p. 655-661.

Research output: Contribution to journalArticle

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