Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer

Archives of Biochemistry and Biophysics

Volumn 494, Issue 1, 2010, Pages 46-57

  Espinoza Fonseca, L Michel ^a,b   Wong Ramírez, Carlos ^b   Trujillo Ferrara, José G ^b  

^a UNIVERSITY OF MINNESOTA   (United States)

^b INSTITUTO POLITÉCNICO NACIONAL   (Mexico)

Author keywords

Aromatic aromatic interactions; Disorder to order transitions; Intrinsically disordered proteins regions; Molecular dynamics simulations; Triosephosphate isomerase

Indexed keywords

CYSTEINE; DIMER; GLYCINE; MONOMER; TRIOSEPHOSPHATE ISOMERASE; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; DISULFIDE BOND; ENZYME CONFORMATION; ENZYME STABILITY; HIGH TEMPERATURE; MOLECULAR DYNAMICS; NONHUMAN; PLASMODIUM FALCIPARUM; PRINCIPAL COMPONENT ANALYSIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PLASMODIUM FALCIPARUM; PROTEIN CONFORMATION; TRIOSE-PHOSPHATE ISOMERASE; TYROSINE;

PLASMODIUM FALCIPARUM;

EID: 74249101059     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.11.009     Document Type: Article

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