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Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
- Source :
- Proceedings of the National Academy of Sciences of the United States of America; February 1994, Vol. 91 Issue: 4 p1515-1518, 4p
- Publication Year :
- 1994
-
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.
Details
- Language :
- English
- ISSN :
- 00278424 and 10916490
- Volume :
- 91
- Issue :
- 4
- Database :
- Supplemental Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Periodical
- Accession number :
- ejs60464921
- Full Text :
- https://doi.org/10.1073/pnas.91.4.1515