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Article

Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution.

Biochemistry - 20 May 2008

Peimbert Mariana, Domínguez-Ramírez Lenin, Fernández-Velasco D Alejandro

Abstract excerpt

Triosephosphate isomerase from Saccharomyces cerevisiae (wt-TIM) is an obligated homodimer. The interface of wt-TIM is formed by 34 residues. In the native dimer, each monomer buries nearly 2600 A(2) of accessible surface area (ASA), and 58.4% of the interface ASA is hydrophobic. We determined the thermodynamic and functional consequences of increasing the hydrophobic character of the wt-TIM interface. Mutations...

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Identifiers

PMID: 18439027
DOI: 10.1021/bi702502k

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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