The stability and kinetics of unfolding and refolding of the P167T mutant of the TEM-1 p-lactamase have been investigated as a function of guanidine hydrochloride concentration. The activity of the mutant enzyme was not significantly modified, which strongly suggests that the Glu166Thr167 peptide bo
β¦ LIBER β¦
PBOND: Web Server for the Prediction of Proline and Non-Proline cis I trans Isomerization
β Scribed by Konstantinos P. Exarchos; Themis P. Exarchos; Costas Papaloukas; Anastassios N. Troganis; Dimitrios I. Fotiadis
- Book ID
- 117802461
- Publisher
- Elsevier Science
- Year
- 2009
- Tongue
- English
- Weight
- 587 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1672-0229
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We wished to test the hypothesis that the non proline cis to trans isomerization of the peptide bond at position 167 in the S. aureus β€-lactamase PC1 exerts a significant controlling effect on the folding pathway of this enzyme. The previous data presented in support of this hypothesis could not rul