Role of arginine 29 and glutamic acid 81 interactions in the conformational stability of human chloride intracellular channel 1

Biochemistry

Volumn 51, Issue 40, 2012, Pages 7854-7862

  Legg E'Silva, Derryn ^a   Achilonu, Ikechukwu ^a   Fanucchi, Sylvia ^a   Stoychev, Stoyan ^a   Fernandes, Manuel ^a   Dirr, Heini W ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

C-DOMAIN; CONFORMATIONAL STABILITIES; FREE ENERGY CHANGE; GLOBAL STRUCTURE; GLUTAMIC ACID; HYDROPHOBIC INTERACTIONS; INTRACELLULAR CHANNEL; ION CHANNEL; MEMBRANE-BOUND; NATIVE STATE; OBSERVATION POINT; PH SENSITIVITY; PHYSIOLOGICAL PH RANGE; SALT BRIDGES; SOLVED CRYSTAL STRUCTURES; SPECTROSCOPIC STUDIES; TWO-STATE; WILD TYPES;

CHLORINE COMPOUNDS; CYTOLOGY; PH; PH SENSORS; PROTEINS; SPECTROSCOPIC ANALYSIS; UREA;

AMINO ACIDS;

ARGININE; CHLORIDE CHANNEL; CHLORIDE INTRACELLULAR CHANNEL 1; GLUTAMIC ACID; UNCLASSIFIED DRUG; UREA;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR STABILITY; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN UNFOLDING;

AMINO ACID SEQUENCE; ARGININE; CHLORIDE CHANNELS; CRYSTALLIZATION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GLUTAMIC ACID; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROMETRY, FLUORESCENCE; X-RAY DIFFRACTION;

EID: 84867449759     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300874b     Document Type: Article

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