BORCHERT, TV and ABAGYAN, R and JAENICKE, R and WIERENGA, RK (1994) DESIGN, CREATION, AND CHARACTERIZATION OF A STABLE, MONOMERIC TRIOSEPHOSPHATE ISOMERASE. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 91 (4). pp. 1515-1518. ISSN 0027-8424,
Full text not available from this repository.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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA-BRUCEI; SUBUNIT INTERFACE; PROTEINS; MUTAGENESIS; ENZYMES; PARAMETERS; EXPRESSION; YEAST; ACIDS; LOOP DELETION; MONOMERIZATION; PROTEIN ENGINEERING |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53458 |
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