Comparative unfolding studies of psychrophilic and mesophilic uracil DNA glycosylase: MD simulations show reduced thermal stability of the cold-adapted enzyme

Journal of Molecular Graphics and Modelling

Volumn 26, Issue 1, 2007, Pages 124-134

  Olufsen, Magne ^a   Brandsdal, Bjørn Olav ^a   Smalås, Arne Oskar ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

Author keywords

Cold adaptation; Molecular dynamics; Protein unfolding; Psychrophilic; Uracil DNA glycosylase

Indexed keywords

CATALYSTS; CRYSTAL STRUCTURE; ENZYME INHIBITION; MOLECULAR DYNAMICS; THERMODYNAMIC STABILITY;

DISTINCT STRUCTURAL; MESOPHILIC ENZYME; PSYCHROPHILIC ENZYME; THERMOSTABILITY;

DNA;

URACIL DNA GLYCOSIDASE;

ARTICLE; COMPARATIVE STUDY; COMPUTER SIMULATION; CONFORMATIONAL TRANSITION; COOLING; ENZYME CONFORMATION; ENZYME STABILITY; EXCISION REPAIR; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN FOLDING; THERMOSTABILITY;

ACCLIMATIZATION; ANIMALS; COLD CLIMATE; COMPUTER SIMULATION; ENZYME STABILITY; GADUS MORHUA; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECIES SPECIFICITY; THERMODYNAMICS; URACIL-DNA GLYCOSIDASE;

GADUS MORHUA;

EID: 34250834398     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2006.10.003     Document Type: Article

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