Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases

Biochemistry

Volumn 46, Issue 41, 2007, Pages 11536-11549

  Gráczer, Éva ^a   Varga, Andrea ^a   Hajdú, István ^a   Melnik, Bogdan ^b   Szilágyi, András ^a   Semisotnov, Gennady ^b   Závodszky, Péter ^a   Vas, Mária ^a  

^a INSTITUTE OF ENZYMOLOGY   (Hungary)

^b INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; COMPLEXATION; MANGANESE; MOLECULAR STRUCTURE; THERMODYNAMIC STABILITY;

COMPLEX STRUCTURE; ISOPROPYLMALATE DEHYDROGENASES (IPMDH); PSYCHROTROPHIC ENZYMES;

PROTEIN FOLDING;

3 ISOPROPYLMALATE DEHYDROGENASE;

ARTICLE; ENZYME BINDING; ENZYME STABILITY; ESCHERICHIA COLI; MESOPHILIC BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STABILITY; SEQUENCE ALIGNMENT; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMUS THERMOPHILUS; VIBRIO;

3-ISOPROPYLMALATE DEHYDROGENASE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; CONSERVED SEQUENCE; DRUG STABILITY; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; THERMODYNAMICS; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS; VIBRIO SP.;

EID: 35348897426     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700754q     Document Type: Article

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