Evidence for light-induced lysine conformational changes during the primary event of the bacteriorhodopsin photocycle

Earl McMaster*, Aaron Lewis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Fourier transform infrared difference spectroscopy is used to examine the role of lysine in the primary event of the bacteriorhodopsin photocycle. Isotopically labeled lysine is used to tentatively assign the lysine modes in the BR and K species. The results suggest that the lysine side-chain undergoes conformational changes in concert with the known light-induced chromophore structural alterations.

Original languageEnglish
Pages (from-to)86-91
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume156
Issue number1
DOIs
StatePublished - 14 Oct 1988
Externally publishedYes

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