Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 1, 2012, Pages 184-193

  Campbell, James C ^a   Whitten, Steven T ^a  

^a Texas State University San Marcos   (United States)

Author keywords

Cold denaturation; Ensemble; m values; Substructures; Unfolding

Indexed keywords

CHYMOTRYPSIN INHIBITOR; NUCLEASE; UBIQUITIN;

ARTICLE; COLD TOLERANCE; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; ROOM TEMPERATURE; SENSITIVITY ANALYSIS; STAPHYLOCOCCACEAE; THERMODYNAMICS;

ALGORITHMS; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; COLD TEMPERATURE; COMPUTER SIMULATION; GUANIDINE; HUMANS; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PEPTIDES; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; UBIQUITIN;

EID: 83555176350     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23178     Document Type: Article

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