STRUCTURE DETERMINATION OF A TETRADECAPEPTIDE MIMICKING THE RXVRG CONSENSUS SEQUENCE RECOGNIZED BY A XENOPUS-LAEVIS SKIN ENDOPROTEASE - AN APPROACH BASED ON SIMULATED ANNEALING AND H-1-NMR

The tetradecapeptide of sequence -Arg(5)-Asp-Val-Arg-Gly(9)-Phe-Ala-Se r-Phe-Leu-NH2 is recognized by a putative maturation endoprotease of t he Xenopus laevis skin, which cleaves between Arg(8) and Gly(9). A con formational search has been performed on this peptide by simulated ann ealing calculations. Two different models in agreement with the NMR da ta 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 ).