Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturants

Biochemistry

Volumn 49, Issue 30, 2010, Pages 6317-6328

  Dutta, Arpana ^a   Tirupula, Kalyan C ^a   Alexiev, Ulrike ^b   Klein Seetharaman, Judith ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL DENATURANTS; CONCENTRATION OF; DENATURED STATE; DENATURING CONDITIONS; FOLDING MECHANISM; G PROTEIN COUPLED RECEPTORS; GUANIDINE HYDROCHLORIDE; HELICAL MEMBRANE; HYDROPHOBIC REGIONS; MAMMALIAN MEMBRANES; MEMBRANE PROTEINS; NON-NATIVE STATE; PRIMARY FUNCTIONS; PROTEIN CONCENTRATIONS; SDS-PAGE; SECONDARY STRUCTURES; SODIUM DODECYL SULFATE; TRIFLUOROACETIC ACIDS;

BIOLOGICAL MEMBRANES; MAMMALS; METABOLISM; SODIUM; SODIUM SULFATE; UREA;

PROTEINS;

DODECYL SULFATE SODIUM; GUANIDINE; RHODOPSIN; TRIFLUOROACETIC ACID; UREA;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

ANIMALS; CATTLE; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GUANIDINE; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; RHODOPSIN; SODIUM DODECYL SULFATE; TRIFLUOROACETIC ACID; UREA;

MAMMALIA;

EID: 77955022753     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100338e     Document Type: Article

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