Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: Reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation

Biochemistry

Volumn 38, Issue 25, 1999, Pages 7938-7944

  Klein Seetharaman, Judith ^a   Hwa, John ^a   Cai, Kewen ^a   Altenbach, Christian ^b   Hubbell, Wayne L ^b   Gobind Khorana, H ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b JULES STEIN EYE INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BLEACHING; CHROMATOPHORE; DERIVATIZATION; DISULFIDE BOND; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CATTLE; CYSTEINE; CYTOPLASM; DARKNESS; DISULFIDES; LIGHT; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRIDINES; RHODOPSIN; SULFHYDRYL REAGENTS; TRANSDUCIN;

EID: 0033594869     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990013t     Document Type: Article

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