Circular dichroism and fluorescence spectroscopy of cysteinyl-tRNA synthetase from Halobacterium salinarum ssp. NRC-1 demonstrates that group I cations are particularly effective in providing structure and stability to this halophilic protein

PLoS ONE

Volumn 9, Issue 3, 2014, Pages

  Reed, Christopher J ^a   Bushnell, Sarah ^a   Evilia, Caryn ^a  

^a Nucl Eng Idaho State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHLORIDE; CATION; CESIUM CHLORIDE; CHLORIDE ION; COPPER CHLORIDE; CYSTEINE TRANSFER RNA LIGASE; LITHIUM CHLORIDE; MAGNESIUM CHLORIDE; METAL ION; NICKEL CHLORIDE; POTASSIUM; POTASSIUM CHLORIDE; RNA LIGASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG; ZINC CHLORIDE; AMINO ACID TRANSFER RNA LIGASE; CYSTEINYL-TRNA SYNTHETASE;

ARTICLE; BACTERIAL STRAIN; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HALOBACTERIUM SALINARUM; MELTING POINT; MOLECULAR INTERACTION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; ULTRAVIOLET RADIATION; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; PROCEDURES; SPECTROFLUOROMETRY;

AMINO ACYL-TRNA SYNTHETASES; CATIONS; CIRCULAR DICHROISM; ENZYME STABILITY; HALOBACTERIUM SALINARUM; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE;

EID: 84897103549     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0089452     Document Type: Article

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