How deep is the potential well confining a protein in a specific conformation? A single-molecule study on temperature dependence of conformational change between 5 and 18 K

Hiroyuki Oikawa, Satoru Fujiyoshi, Takehisa Dewa, Mamoru Nango, Michio Matsushita

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

The fluorescence excitation spectrum of a single chromophore molecule in a photosynthetic pigment-protein complex is known to change in time at liquid helium temperature. The spectral change reflects a conformational change of the protein to which the chromophore binds. This work follows the temporal behavior of the spectrum of a single chromophore in the temperature range between 5 adn 18 K. The temperature dependence reveals two types of conformational change of the protein, i.e., thermally activated motions over a potential barrier of ca. 0.1 kJ/mol and temperature-independent motions of tunneling of a proton.

Original languageEnglish
Pages (from-to)4580-4581
Number of pages2
JournalJournal of the American Chemical Society
Volume130
Issue number14
DOIs
Publication statusPublished - 2008 Apr 9
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)

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