Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels

Biochemistry

Volumn 35, Issue 45, 1996, Pages 14040-14046

  Yang, Ke ^a,c   Farrens, David L ^a,d   Altenbach, Christian ^b   Farahbakhsh, Zohreh T ^b   Hubbell, Wayne L ^b   Gobind Khorana, H ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b JULES STEIN EYE INSTITUTE   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^d OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; DISULFIDE BOND; GENE MUTATION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CYSTEINE; DISULFIDES; DNA MUTATIONAL ANALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; RHODOPSIN; SULFHYDRYL COMPOUNDS; THERMOLYSIN;

ANIMALIA;

EID: 0029680797     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962113u     Document Type: Article

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