Výsledky vyhledávání - "Francois-Regis Chalaoux"

Two-Dimensional1H NMR Study of a Tetradecapeptide with the Consensus Sequence Arg5-Asp-Val-Arg-Gly9: Structural Effects of the Outside Substitution Ser12by Ala12

Autor: Francois-Regis Chalaoux, Jacques Riand, Anne-Marie Leseney, Daniel Baron

Publikováno v: Journal of Biomolecular Structure and Dynamics. 12:993-1008

Conformation of a tetradecapeptide with a RXVRG consensus sequence, Arg5-Asp-Val-Arg-Gly9, found in several precursors of antibacterian peptides, was investigated in dimethylsulfoxide solution by proton NMR spectroscopy. Complete resonance assignment

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06308f3c38a6b874abc6f789f9830f56
https://doi.org/10.1080/07391102.1995.10508792

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NMR conformational study of a model tetradecapeptide mimicking the RXVRG consensus cleavage site of a Xenopus laevis skin endoprotease

Autor: Daniel Baron, Anne-Marie Leseney, Francois-Regis Chalaoux, Jacques Riand

Publikováno v: International journal of peptide and protein research. 45(6)

A model tetradecapeptide, used for the purification of the RXVRG-endoprotease from Xenopus laevis skin exudate, has been studied by two-dimensional NMR, correlation (COSY) and NOE (NOESY) spectroscopy. This peptide has the 5-9 consensus sequence (RXV

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::932a10b527b638c273ba6f831f6347a5
https://pubmed.ncbi.nlm.nih.gov/7558582

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Structure determination of a tetradecapeptide mimicking the RXVRG consensus sequence recognized by a Xenopus laevis skin endoprotease: an approach based on simulated annealing and 1H NMR

Autor: Daniel Baron, P. Vigny, Sonja Meddeb, Jean-Philippe Demaret, Francois-Regis Chalaoux, Jean-Pierre Ballini

Publikováno v: Journal of computer-aided molecular design. 9(2)

The tetradecapeptide of sequence H-Asp-Val-Asp-Glu-Arg 5-Asp-Val-Arg-Gly9-Phe-Ala-Ser-Phe-Leu-NH2 is recognized by a putative maturation endoprotease of the Xenopus laevis skin, which cleaves between Arg8 and Gly9. A conformational search has been pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0d5dae85033efb89bafe3a3c670e580
https://pubmed.ncbi.nlm.nih.gov/7608747

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Conformational studies of an undecapeptide reproducing the consensus sequence around the cleavage site of the RXVRG endoprotease from Xenopus laevis skin

Autor: Anne-Marie Leseney, Francois-Regis Chalaoux, Daniel Baron, Jacques Riand

Publikováno v: Biopolymers. 34(10)

Two synthetic fragments, corresponding to the 4–9 and 4–14 sequences of a tetradecapeptide used as a model to test the RXVRG-endoprotease activity from Xenopus laevis skin, have been studied by two-dimensional nmr spectroscopies, correlated spect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::419b7a76c3030ab672ca4ec116e26ac7
https://pubmed.ncbi.nlm.nih.gov/7948725

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