Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase: The role of conserved residues and complementary mutations

FEBS Journal

Volumn 276, Issue 15, 2009, Pages 4169-4183

  Banerjee, Mousumi ^a   Balaram, Hemalatha ^b   Balaram, Padmanabhan ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

Author keywords

Aromatic cluster; Dimer stability; Plasmodium falciparum; Subunit interface; Triosephosphate isomerase

Indexed keywords

GUANIDINE; MUTANT PROTEIN; PROTEIN WT; PROTEIN Y74W; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; UREA;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; GEL FILTRATION; GIARDIA LAMBLIA; KINETICS; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN FOLDING;

AMINO ACID SUBSTITUTION; ANIMALS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DIMERIZATION; GENETIC VARIATION; GLYCOLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PLASMODIUM FALCIPARUM; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTOZOAN PROTEINS; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI;

GIARDIA INTESTINALIS; PLASMODIUM FALCIPARUM;

EID: 68149124204     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07126.x     Document Type: Article

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