Thermostabilization of Bacillus circulans xylanase: Computational optimization of unstable residues based on thermal fluctuation analysis

Journal of Biotechnology

Volumn 151, Issue 1, 2011, Pages 56-65

  Joo, Jeong Chan ^a   Pack, Seung Pil ^b   Kim, Yong Hwan ^c   Yoo, Young Je ^a  

^a Seoul National University   (South Korea)

^b Korea University   (South Korea)

^c Kwangwoon University   (South Korea)

Author keywords

Computational design; Flexibility; Molecular dynamics simulation; Protein engineering; Thermostability; Xylanase

Indexed keywords

COMPUTATIONAL DESIGN; FLEXIBILITY; MOLECULAR DYNAMICS SIMULATION; PROTEIN ENGINEERING; THERMOSTABILITY; XYLANASES;

BACTERIOLOGY; BIOCHEMICAL ENGINEERING; CATALYSTS; DESIGN; ENZYMES; GENETIC ENGINEERING; HIGH TEMPERATURE APPLICATIONS; MOLECULAR MECHANICS; OPTIMIZATION;

MOLECULAR DYNAMICS;

MUTANT PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ARTICLE; BACILLUS CIRCULANS; CONTROLLED STUDY; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HIGH TEMPERATURE; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR MODEL; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROCESS OPTIMIZATION; SIMULATION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACIDS; BACILLUS; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; HOT TEMPERATURE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

BACILLUS CIRCULANS;

EID: 78650678219     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.10.002     Document Type: Article

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