Thermodynamic characterization of yeast triosephosphate isomerase refolding: Insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme

Biochemical Journal

Volumn 370, Issue 3, 2003, Pages 785-792

  Nájera, Hugo ^a   Costas, Miguel ^a,b   Fernández Velasco, D Alejandro ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

Dimer evolution; Equilibrium; Hysteresis; Monomeric intermediate; TIM barrel; Unfolding refolding

Indexed keywords

CATALYST ACTIVITY; COMPUTER SIMULATION; OLIGOMERS; SPECTROSCOPIC ANALYSIS; THERMODYNAMICS;

REVERSIBLE DENATURATION;

PROTEINS;

ENZYME; GUANIDINE; MONOMER; OLIGOMER; TRIOSEPHOSPHATE ISOMERASE; UREA;

ARTICLE; CALCULATION; CATALYSIS; CONTROLLED STUDY; DATA ANALYSIS; DISSOCIATION; ELUTION; ENERGY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME KINETICS; ENZYME RENATURATION; HYDRODYNAMICS; HYSTERESIS; MEDICAL LITERATURE; NONHUMAN; PRIORITY JOURNAL; PROCESSING; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE; SIMULATION; SPECIES; SPECTROSCOPY; TECHNIQUE; THERMODYNAMICS; THERMOSTABILITY;

ANIMALS; ENZYME STABILITY; GUANIDINE; HUMANS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRIOSE-PHOSPHATE ISOMERASE;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0037444807     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021439     Document Type: Article

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