Engineering of a stable mutant malic enzyme by introducing an extra ion- pair to the protein

Proteins: Structure, Function and Genetics

Volumn 31, Issue 1, 1998, Pages 61-73

  Huang, Shih Ming ^a   Chou, Wei Yuan ^a   Lin, Shu Iu ^a   Chang, Gu Gang ^a  

^a NATIONAL DEFENSE MEDICAL CENTER   (Taiwan)

Author keywords

Malic enzyme; Mutagenesis; Protein folding; Protein stability; Salt bridge

Indexed keywords

ARGININE; GLUTAMIC ACID; ION; LIVER ENZYME; LYSINE; MALATE DEHYDROGENASE (DECARBOXYLATING); METHIONINE; MUTANT PROTEIN; UREA;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GENETIC ENGINEERING; NONHUMAN; PIGEON; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; COLUMBIDAE; HEAT; IONS; KINETICS; LIVER; MALATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; UREA;

ANIMALIA; COLUMBA; FELIS CATUS;

EID: 0032054520     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980401)31:1<61::AID-PROT6>3.0.CO;2-K     Document Type: Article

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