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. 1994 Feb 15;91(4):1515–1518. doi: 10.1073/pnas.91.4.1515

Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.

T V Borchert 1, R Abagyan 1, R Jaenicke 1, R K Wierenga 1
PMCID: PMC43190  PMID: 8108439

Abstract

Protein engineering on trypanosomal triosephosphate isomerase (TIM) converted this oligomeric enzyme into a stable, monomeric protein that is enzymatically active. Wild-type TIM consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit. By replacing 15 residues of the major interface loop by another 8-residue fragment, a variant was constructed that is a stable and monomeric protein with TIM activity. The length, sequence, and conformation of the designed fragment were suggested by extensive modeling.

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Selected References

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