Role of residual structure in the unfolded state of a thermophilic protein

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 20, 2003, Pages 11345-11349

  Robic, Srebrenka ^a   Guzman Casado, Mercedes ^b   Sanchez Ruiz, Jose M ^b   Marqusee, Susan ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF GRANADA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; RIBONUCLEASE H; THERMOPHILIC PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; MELTING POINT; MUTAGENICITY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMAL ANALYSIS; THERMODYNAMICS; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; MODELS, MOLECULAR; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE H, CALF THYMUS; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; THERMUS; THERMUS THERMOPHILUS;

EID: 0141816814     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.1635051100     Document Type: Article

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