Site-specific mutations provide new insights into the origin of pH effects and alternative spectral forms in the photoactive yellow protein from Halorhodospira halophila

Biochemistry

Volumn 42, Issue 11, 2003, Pages 3319-3325

  Meyer, T E ^a   Devanathan, S ^a   Woo, T ^b   Getzoff, E D ^b   Tollin, G ^a   Cusanovich, M A ^a  

^a University of Arizona   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDITY; ALKALINITY; HYDROGEN BONDS; HYDROLYSIS; PH EFFECTS; TITRATION;

SITE-SPECIFIC MUTATIONS;

PROTEINS;

4 HYDROXYCINNAMYLCYSTEINE; ANION; CARBOXYL GROUP; CARBOXYLIC ACID DERIVATIVE; CYSTEINE DERIVATIVE; PHOTOACTIVE YELLOW PROTEIN; SOLVENT; THIOCYANATE; UNCLASSIFIED DRUG; WATER;

ACID BASE BALANCE; ARTICLE; CHROMATOPHORE; HYDROGEN BOND; HYDROLYSIS; IONIZATION; PH; PHOTOTROPHIC BACTERIUM; PRECIPITATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; TITRIMETRY;

AMINO ACIDS; BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; HEAT; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; PHOTORECEPTORS, MICROBIAL; PROTEIN DENATURATION; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); HALOPHILA; HALORHODOSPIRA; HALORHODOSPIRA HALOPHILA; PHOTOBACTERIA;

EID: 0037465835     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020702w     Document Type: Article

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