Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride

Spectroscopy

Volumn 24, Issue 3-4, 2010, Pages 367-373

  Stepanenko, Olesya V ^a   Kuznetsova, Irina M ^a   Verkhusha, Vladislav V ^b   Staiano, Maria ^c   D'Auria, Sabato ^c   Turoverov, Konstantin K ^a  

^a INSTITUTE OF CYTOLOGY   (Russian Federation)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

fluorescent proteins; folding of proteins with beta barrel topology; Odorant binding proteins; protein stability; small guanidine hydrochloride concentrations

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CHROMOPHORES; FLUORESCENCE; ODORS; TOPOLOGY;

FLUORESCENT PROTEIN; FOLDING OF PROTEINS WITH BETA-BARREL TOPOLOGIES; GUANIDINE HYDROCHLORIDE; MICROENVIRONMENTS; ODORANT-BINDING PROTEINS; PROTEIN STABILITY; SMALL GUANIDINE HYDROCHLORIDE CONCENTRATIONS; STRUCTURAL DISTURBANCES; TRYPTOPHAN RESIDUES; Β-BARREL;

PROTEINS;

CHLORIDE; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PORCINE ODORANT BINDING PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CHROMATOPHORE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

EID: 77954777045     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2010/935656     Document Type: Article

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