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Volumn 52, Issue 7, 2013, Pages 1959-1963

Engineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel

Author keywords

directed evolution; enzyme catalysis; enzymes; protein engineering; protein stability

Indexed keywords

COSOLVENT MOLECULES; COSOLVENTS; DIRECTED EVOLUTION; ENZYME CATALYSIS; ENZYME STABILITY; KEY DETERMINANTS; PROTEIN CRYSTALLOGRAPHY; PROTEIN ENGINEERING; PROTEIN STABILITY;

EID: 84873532872     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201206708     Document Type: Article
Times cited : (115)

References (39)
  • 22
    • 0003760238 scopus 로고
    • 0.5 is the substrate concentration at which half-maximal velocity is achieved according to the cooperativity model; see the Supporting Information methods. Kinetic parameters were determined in mixtures of 60 m M glycine buffer (pH 8.6) with 40 % (v/v) DMSO at 37 °C
    • 0.5 is the substrate concentration at which half-maximal velocity is achieved according to the cooperativity model; see the Supporting Information methods. Kinetic parameters were determined in mixtures of 60 m M glycine buffer (pH 8.6) with 40 % (v/v) DMSO at 37 °C.
    • (1993) Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems
    • Segel, I.H.1
  • 32
    • 84868156224 scopus 로고    scopus 로고
    • the Supporting Information
    • E. Chovancova, et al., PLoS Comput. Biol. 2012, 8, e 1002708, see the Supporting Information
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002708
    • Chovancova, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.