Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima

Protein Engineering

Volumn 13, Issue 7, 2000, Pages 501-507

  Consalvi, Valerio ^a   Chiaraluce, Roberta ^a   Giangiacomo, Laura ^a   Scandurra, Roberto ^a   Christova, Petya ^b   Karshikoff, Andrej ^c   Knapp, Stefan ^d   Ladenstein, Rudolf ^c  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b BULGARIAN ACADEMY OF SCIENCES   (Bulgaria)

^c KAROLINSKA INSTITUTE   (Sweden)

^d Pharmacia U   (Italy)

Author keywords

Domain; Glutamate dehydrogenase; Hyperthermophiles; Protein; Thermodynamic stability

Indexed keywords

GLUTAMATE DEHYDROGENASE; GUANIDINE; RECOMBINANT ENZYME;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; ENZYME CONFORMATION; ESCHERICHIA COLI; MELTING POINT; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; TEMPERATURE; TEMPERATURE DEPENDENCE; THERMODYNAMICS; THERMOPHILIC BACTERIUM; THERMOTOGA MARITIMA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; THERMOTOGA MARITIMA;

EID: 0033858185     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/13.7.501     Document Type: Article

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