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Article

Water and peptide backbone structure in the active center of bovine rhodopsin.

Biochemistry - 20 May 1997

Nagata T, Terakita A, Kandori H, Kojima D, Shichida Y, Maeda A

Abstract excerpt

Difference FTIR spectra in the conversion of rhodopsin or isorhodopsin to bathorhodopsin were recorded for recombinant wild-type and E113Q bovine rhodopsins. Differences in various vibrational modes between E113Q and the wild-type proteins whose Schiff bases interact with chloride and Glu113, respectively, were analyzed. Water molecules in rhodopsin that change upon formation of bathorhodopsin are detected by a...

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PMID: 9166788
DOI: 10.1021/bi962920t

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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