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Article

Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes

1 Oct 1998

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9761683
DOI: 10.1006/jmbi.1998.2094

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Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomesPMID 9761683Read ↗

The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes.Semantic proximity Read ↗

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Key residues of loop 3 in the interaction with the interface residue at position 14 in triosephosphate isomerase from Trypanosoma brucei.Semantic proximity Read ↗

Molecular and biochemical characterization of novel glucokinases from Trypanosoma cruzi and Leishmania spp.Semantic proximity Read ↗

Differences in Energy Metabolism Between TrypanosomatidaeSemantic proximity Read ↗

The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.Semantic proximity Read ↗

A strategy based on thermal flexibility to design triosephosphate isomerase proteins with increased or decreased kinetic stability.Semantic proximity Read ↗

Structural and thermodynamic folding characterization of triosephosphate isomerases from Trichomonas vaginalis reveals the role of destabilizing mutations following gene duplication.Semantic proximity Read ↗

Different strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution.Semantic proximity Read ↗

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