Thermostabilizing mutations preferentially occur at structural weak spots with a high mutation ratio

Journal of Biotechnology

Volumn 159, Issue 3, 2012, Pages 135-144

  Rathi, Prakash C ^a   Radestock, Sebastian ^a   Gohlke, Holger ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Citrate synthase; Constraint network analysis; Flexibility; Protein engineering; Rigidity theory; Thermostability

Indexed keywords

CITRATE SYNTHASE; CONSTRAINT NETWORKS; FLEXIBILITY; PROTEIN ENGINEERING; THERMOSTABILITY;

AMINO ACIDS; BIOCHEMICAL ENGINEERING; GENETIC ENGINEERING; RIGIDITY;

HYDROPHOBICITY;

CITRATE SYNTHASE;

AMINO ACID SEQUENCE; ARTICLE; HYDROGEN BOND; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN STRUCTURE; TEMPERATURE; THERMOSTABILITY;

ANIMALS; ARCHAEAL PROTEINS; CITRATE (SI)-SYNTHASE; DATABASES, PROTEIN; ENZYME STABILITY; HOT TEMPERATURE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR DYNAMICS SIMULATION; MUTATION; PROTEIN ENGINEERING; PROTEIN UNFOLDING; PROTEINS; REPRODUCIBILITY OF RESULTS; SWINE;

EID: 84860835198     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2012.01.027     Document Type: Article

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