Structural and energetic basis of protein kinetic destabilization in human phosphoglycerate kinase 1 deficiency

Biochemistry

Volumn 52, Issue 7, 2013, Pages 1160-1170

  Pey, Angel L ^a   Mesa Torres, Noel ^a   Chiarelli, Laurent R ^b   Valentini, Giovanna ^b  

^a UNIVERSITY OF GRANADA   (Spain)

^b UNIVERSITY OF PAVIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

COMMON FEATURES; ENTROPIC CONTRIBUTIONS; GENETIC DISEASE; HAMMOND EFFECT; HUMAN GENETIC DISEASE; IRREVERSIBLE DENATURATION; KINETIC ANALYSIS; KINETIC CONTROL; KINETIC STABILITY; KINETIC STABILIZATION; MUTANT ENZYMES; NATIVE STATE; PHOSPHOGLYCERATE KINASE; PHYSIOLOGICAL TEMPERATURE; PROTEIN KINETICS; SOLVENT EXPOSURE; THERMAL DENATURATIONS; TIME-SCALES; TRANSITION STATE; TWO-STATE; WILD TYPES;

DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYMES; PROTEINS; THERMODYNAMIC STABILITY; UREA;

KINETICS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE KINASE 1; SOLVENT; UNCLASSIFIED DRUG; UREA;

ARTICLE; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ENTROPY; ENZYME ANALYSIS; ENZYME DEFICIENCY; ENZYME DENATURATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; GENE MUTATION; IN VITRO STUDY; PHOSPHOGLYCERATE KINASE 1 DEFICIENCY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN UNFOLDING; TEMPERATURE; THERMODYNAMICS; THERMOSTABILITY; WILD TYPE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CALORIMETRY, DIFFERENTIAL SCANNING; ENZYME STABILITY; GENETIC DISEASES, X-LINKED; HUMANS; KINETICS; METABOLISM, INBORN ERRORS; MODELS, CHEMICAL; MUTATION; PHOSPHOGLYCERATE KINASE; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE; UREA;

EID: 84874101765     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301565m     Document Type: Article

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