Unusual effect of salts on the homodimeric structure of NADH oxidase from Thermus thermophilus in acidic pH

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 1, 2006, Pages 129-137

  Stupák, Marek ^a   Žoldák, Gabriel ^a   Musatov, Andrej ^b   Sprinzl, Mathias ^c   Sedlák, Erik ^a  

^a P J AFÁRIK UNIVERSITY   (Slovakia)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^c UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Circular dichroism; Dimeric interface; Flavoprotein; Molten globule; NADH oxidase

Indexed keywords

AMMONIUM CHLORIDE; CESIUM CHLORIDE; FLAVOPROTEIN; HOMODIMER; LITHIUM CHLORIDE; POTASSIUM CHLORIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SODIUM CHLORIDE; SODIUM PERCHLORATE;

ACIDITY; ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STRUCTURE; IONIC STRENGTH; MELTING POINT; PH; PKA; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SEDIMENTATION RATE; THERMUS THERMOPHILUS;

DIMERIZATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MULTIENZYME COMPLEXES; NADH, NADPH OXIDOREDUCTASES; OSMOLAR CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SODIUM CHLORIDE; TEMPERATURE; THERMODYNAMICS; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 33644835559     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.10.020     Document Type: Article

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