Improving the thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 using a computationally aided method

Applied Microbiology and Biotechnology

Volumn 97, Issue 7, 2013, Pages 2997-3006

  Tian, Jian ^a   Wang, Ping ^a   Huang, Lu ^a   Chu, Xiaoyu ^a   Wu, Ningfeng ^a   Fan, Yunliu ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Methyl parathion hydrolase; Prethermut; Site evolutionary entropy; Thermostability; Unfolding free energy

Indexed keywords

EVOLUTIONARY APPROACH; FREE-ENERGY DIFFERENCE; METHYL PARATHION HYDROLASE; PRETHERMUT; PROTEIN THERMAL STABILITY; PROTEIN THERMOSTABILITIES; SATURATION MUTAGENESIS; THERMOSTABILITY;

AMINO ACIDS; ENTROPY; FREE ENERGY; GENETIC ENGINEERING; HYDROLASES; LIBRARIES; THERMODYNAMIC STABILITY;

PROTEINS;

PARATHION METHYL;

AMINO ACID; BACTERIUM; BIOENGINEERING; ENTROPY; ENZYME ACTIVITY; MUTATION; PREDICTION; PROTEIN; THERMODYNAMIC PROPERTY;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENTROPY; ENZYME DEGRADATION; NONHUMAN; NUCLEOTIDE SEQUENCE; OCHROBACTRUM; POINT MUTATION; PROTEIN ENGINEERING; THERMOSTABILITY; WILD TYPE;

COMPUTER SIMULATION; DNA MUTATIONAL ANALYSIS; ENZYME STABILITY; METHYL PARATHION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; OCHROBACTRUM; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STABILITY; TEMPERATURE;

OCHROBACTRUM SP.;

EID: 84876681671     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4411-7     Document Type: Article

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