Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions

Biochemistry

Volumn 38, Issue 46, 1999, Pages 15380-15387

  Chen, Guo Qiang ^a   Gouaux, Eric ^a  

^a Columbia University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 2 HYDROXY 1 PROPANESULFONIC ACID; BACTERIORHODOPSIN; DODECYL SULFATE SODIUM; PHOSPHORYLCHOLINE;

ARTICLE; ESCHERICHIA COLI; GENE MUTATION; GENE OVEREXPRESSION; HALOBACTERIUM SALINARUM; MICELLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; BACTERIORHODOPSINS; CHOLIC ACIDS; DETERGENTS; DIMYRISTOYLPHOSPHATIDYLCHOLINE; GUANIDINE; HALOBACTERIUM SALINARUM; HYDROGEN-ION CONCENTRATION; MICELLES; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SODIUM DODECYL SULFATE; SOLUTIONS; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; UREA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HALOBACTERIUM SALINARUM; NEGIBACTERIA;

EID: 0001041988     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9909039     Document Type: Article

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