BORCHERT, TV and ZEELEN, JP and SCHLIEBS, W and CALLENS, M and MINKE, W and JAENICKE, R and WIERENGA, RK (1995) AN INTERFACE POINT-MUTATION VARIANT OF TRIOSEPHOSPHATE ISOMERASE IS COMPACTLY FOLDED AND MONOMERIC AT LOW-PROTEIN CONCENTRATIONS. FEBS LETTERS, 367 (3). pp. 315-318. ISSN 1873-3468,
Full text not available from this repository.Abstract
Wild-type trypanosomal triosephosphate isomerase (wtTIM) is a very tight dimer, The interface residue His-47 of wtTIM has been mutated into an asparagine, Ultracentrifugation data show that this variant (H47N) only dimerises at protein concentrations above 3 mg/ml, H47N has been characterised at a protein concentration,where it is predominantly a monomer, Circular dichroism measurements in the near-UV and far-UV show that this monomer is a compactly folded protein with secondary structure similar as in wtTIM. The thermal stability of the monomeric H47N is decreased compared to wtTIM: temperature gradient gel electrophoresis (TGGE) measurements give T-m-values of 41 degrees C for wtTIM, whereas the T-m-value for the monomeric form of H47N is approximately 7 degrees C lower.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ENZYME; DIMER; TRIOSEPHOSPHATE ISOMERASE; INTERFACE; ULTRACENTRIFUGATION; MONOMER; POINT MUTATION |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52438 |
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