Global analysis of the thermal and chemical denaturation of the N- terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, δH°, δS°, and δC(p)/°, and evaluation of solvent isotope effects

Protein Science

Volumn 7, Issue 11, 1998, Pages 2405-2412

  Kuhlman, Brian ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

L9; Protein denaturation; Protein thermodynamics; Solvent isotope effects; Thermophilic proteins

Indexed keywords

DEUTERIUM OXIDE; ISOTOPE; PROTEIN L 9; RIBOSOME PROTEIN; SOLVENT; UNCLASSIFIED DRUG; WATER;

ARTICLE; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0031765187     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071118     Document Type: Article

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