Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
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.

Bibliography

Borchert, T. V., Abagyan, R., Jaenicke, R., & Wierenga, R. K. (1994). Design, creation, and characterization of a stable,monomeric triosephosphate isomerase. Proceedings of the National Academy of Sciences, 91(4), 1515–1518.

Authors 4
  1. T V Borchert (first)
  2. R Abagyan (additional)
  3. R Jaenicke (additional)
  4. R K Wierenga (additional)
References 0 Referenced 97

None

Dates
Type When
Created 19 years, 2 months ago (May 31, 2006, 9:03 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 1:48 p.m.)
Indexed 1 month, 1 week ago (July 19, 2025, 11:21 p.m.)
Issued 31 years, 6 months ago (Feb. 15, 1994)
Published 31 years, 6 months ago (Feb. 15, 1994)
Published Online 31 years, 6 months ago (Feb. 15, 1994)
Published Print 31 years, 6 months ago (Feb. 15, 1994)
Funders 0

None

@article{Borchert_1994, title={Design, creation, and characterization of a stable,monomeric triosephosphate isomerase.}, volume={91}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.91.4.1515}, DOI={10.1073/pnas.91.4.1515}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Borchert, T V and Abagyan, R and Jaenicke, R and Wierenga, R K}, year={1994}, month=feb, pages={1515–1518} }