Restriction of motion of protein side chains during the photocycle of bacteriorhodopsin.

J. Czégé, A. Dér, L. Zimányi, L. Keszthelyi

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Linear dichroism was measured during the photocycle of bacteriorhodopsin. The anisotropy of the sample was produced by the photoselection method. The measurements on purple membrane fragments embedded in agar gel were performed at room temperature with 200 microseconds time resolution at several wavelengths in the 240- to 550-nm spectral region. The induced anisotropy of the retinal chromophore remained constant after the formation of the photocycle intermediate M. The anisotropy was also time independent at the characteristic peaks of the UV absorption change. These experimental data suggest that the direction of the retinal transition dipole moment remains unchanged. Moreover, the affected aromatic protein side chains also do not show any rotational motion when they are in the perturbed or ground states during the photocycle. Our data render it possible to calculate the restricted range of sudden chromophore rotations that might be coupled to the appearance and decay of the M intermediate.

Original languageEnglish
Pages (from-to)7273-7277
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number23
Publication statusPublished - Dec 1982

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Bacteriorhodopsins
Anisotropy
Purple Membrane
Proteins
Agar
Gels
Temperature

ASJC Scopus subject areas

  • General
  • Genetics

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Restriction of motion of protein side chains during the photocycle of bacteriorhodopsin. / Czégé, J.; Dér, A.; Zimányi, L.; Keszthelyi, L.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 79, No. 23, 12.1982, p. 7273-7277.

Research output: Contribution to journalArticle

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