Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: restoration of stability by disulfide cross-linking of subunits.

Gopal, B; Ray, S S; Gokhale, R S; Balaram, H; Murthy, M R; Balaram, P

Gopal, B; Ray, S S; Gokhale, R S; Balaram, H; Murthy, M R; Balaram, P.

Affiliation

Gopal B; Molecular Biophysics Unit, Indian Institute of Science, Bangalore.

Biochemistry ; 38(1): 478-86, 1999 Jan 05.

Article in En | MEDLINE | ID: mdl-9890931

Subject(s)

Cross-Linking Reagents/chemistry; Disulfides/chemistry; Mutagenesis, Site-Directed; Plasmodium falciparum/enzymology; Triose-Phosphate Isomerase/chemistry; Triose-Phosphate Isomerase/genetics; Animals; Chemical Precipitation; Circular Dichroism; Computer Simulation; Crystallography, X-Ray; Cysteine/genetics; Dimerization; Enzyme Activation/genetics; Enzyme Stability/genetics; Models, Molecular; Plasmodium falciparum/genetics; Protein Engineering; Recombinant Proteins/chemistry; Tyrosine/genetics

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Collection: 01-internacional Database: MEDLINE Main subject: Plasmodium falciparum / Triose-Phosphate Isomerase / Mutagenesis, Site-Directed / Cross-Linking Reagents / Disulfides Limits: Animals Language: En Journal: Biochemistry Year: 1999 Document type: Article Country of publication: United States

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