Conserved quantitative stability/flexibility relationships (QSFR) in an orthologous RNase H pair

Proteins: Structure, Function and Genetics

Volumn 62, Issue 1, 2006, Pages 130-143

  Livesay, Dennis R ^a   Jacobs, Donald J ^b,c  

^a CALIFORNIA POLYTECHNIC STATE UNIVERSITY   (United States)

^b CALIFORNIA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF NORTH CAROLINA AT CHARLOTTE   (United States)

Author keywords

Free energy landscape; Molecular cooperativity; Network rigidity; Protein flexibility; Protein stability; RNase H

Indexed keywords

RIBONUCLEASE;

ARTICLE; CATALYSIS; ENTHALPY; GENETIC CONSERVATION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; QUANTITATIVE STABILITY FLEXIBILITY RELATIONSHIP; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYME STABILITY; MODELS, MOLECULAR; PROTEIN CONFORMATION; RIBONUCLEASE H, CALF THYMUS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 30344476409     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20745     Document Type: Article

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