Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange

Biochemistry

Volumn 44, Issue 21, 2005, Pages 7644-7655

  Laurents, Douglas V ^a   Scholtz, J Martin ^b   Rico, Manuel ^a   Pace, C Nick ^b   Bruix, Marta ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b TEXAS A M COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; HYDROGEN EXCHANGE; RIBONUCLEASE SA; THERMAL DENATURATION;

CONFORMATIONS; HYDROGEN; ION EXCHANGE; NUCLEAR MAGNETIC RESONANCE; RNA; SALTS; SPECTROSCOPIC ANALYSIS; THERMAL EFFECTS;

ENZYMES;

AMIDE; DISULFIDE; HYDROGEN; RIBONUCLEASE; SODIUM CHLORIDE; WATER;

ANION EXCHANGE; ARTICLE; DENATURATION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; EXPOSURE; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE IMAGING; PH; PRIORITY JOURNAL; PROTEIN STABILITY; RESIDUE ANALYSIS; SPECTROSCOPY; TEMPERATURE;

AMIDES; DEUTERIUM EXCHANGE MEASUREMENT; DISULFIDES; ELECTROSTATICS; ENZYME STABILITY; GUANIDINE; HEAT; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTONS; RIBONUCLEASES; SODIUM CHLORIDE; STREPTOMYCES AUREOFACIENS; THERMODYNAMICS;

EID: 19644364347     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050142b     Document Type: Article

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