cis-trans-Isomerisation of the proline-peptide-bond in a cyclic tetrapeptide related to chlamydocin
β Scribed by Ernst Haslinger; Hermann Kalchhauser; Peter Wolschann
- Book ID
- 105079476
- Publisher
- Springer Vienna
- Year
- 1984
- Tongue
- English
- Weight
- 174 KB
- Volume
- 115
- Category
- Article
- ISSN
- 0026-9247
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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
The cyclic hexapeptide cycle[ -Pro'-Gly2-Glu3 (OBzl) -Pro4-Phe5-Leu6-] ( 1 ; OBzl: benzyl ester) was modeled and synthesized to be used as a chiral site for the separation of enantiomers. Total correlation spectroscopy and nuclear Ovehauser effect spectroscopy spectra of the peptide in CDCIB showed
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