✦ LIBER ✦
Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by aXenopus laevisskin endoprotease: An approach based on simulated annealing and1H NMR
✍ Scribed by Sonja Meddeb; François-Regis Chalaoux; Jean-Pierre Ballini; Daniel Baron; Paul Vigny; Jean-Philippe Demaret
- Publisher
- Springer Netherlands
- Year
- 1995
- Tongue
- English
- Weight
- 790 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0920-654X
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✦ Synopsis
The tetradecapeptide of sequence H-Asp-Val-Asp-Glu-ArgS-Asp-Val-Arg-Glyg-Phe-Ala-Ser-Phe-Leu-NH2 is recognized by a putative maturation endoprotease of the Xenopus laevis skin, which cleaves between Arg 8 and Gly 9. A conformational search has been performed on this peptide by simulated annealing calculations. Two different models in agreement with the NMR data were found. The conformational difference between the two types of model is located in the consensus sequence, i.e., from Arg 5 to Gly 9.