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  • Title: Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
    Author: Borchert TV, Abagyan R, Jaenicke R, Wierenga RK.
    Journal: Proc Natl Acad Sci U S A; 1994 Feb 15; 91(4):1515-8. PubMed ID: 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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