999 resultados para Librairie de nonapeptides


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[1. ptie.] Vente aura lieu le 29 mars 1870 -- 2. ptie. Vente le 4 mars 1872.

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017.4 T22d v.1 cop.1: Publisher's printed wraps bound-in; "O-7-30" inscribed in blue pencil on front cover; bookseller's label on front cover: "Libreria di Ulrico Hoepli, succ. a Teodoro Laengner, Galleria de Christoforis 15, 60, Milano."

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Issued as premium (forming one vol. per year) to subscribers of the Courrier de la librairie, which was discontinued in 1859, the work extending to Dubuisson only.

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Bulletin d'annonces issued with each number and appended to bound volumes.

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Mode of access: Internet.

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Mode of access: Internet.

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Mémoire numérisé par la Direction des bibliothèques de l'Université de Montréal.

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Mémoire numérisé par la Direction des bibliothèques de l'Université de Montréal.

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Thèse décrivant l'écriture d'outils spécialisés facilitant l'analyse de grandes quantités de données provenant de technologie de séquencage haut débit.

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The conformational properties of foldamers generated from alpha gamma hybrid peptide sequences have been probed in the model sequence Boc-Aib-Gpn-Aib-Gpn-NHMe. The choice of alpha-aminoisobutyryl (Aib) and gabapentin (Gpn) residues greatly restricts sterically accessible coil formational space. This model sequence was anticipated to be a short segment of the alpha gamma C-12 helix, stabilized by three successive 4 -> 1 hydrogen bonds, corresponding to a backbone-expanded analogue of the alpha polypeptide 3(10)-helix. Unexpectedly, three distinct crystalline polymorphs were characterized in the solid state by X-ray diffraction. In one form, two successive C-12 hydrogen bonds were obtained at the N-terminus, while a novel C-17 hydrogen-bonded gamma alpha gamma turn was observed at the C-terminus. In the other two polymorphs, isolated C-9 and C-7 hydrogen-bonded turns were observed at Gpn (2) and Gpn (4). Isolated C-12 and C-9 turns were also crystallographically established in the peptides Boc-Aib-Gpn-Aib-OMe and Boc-Gpn-Aib-NHMe, respectively. Selective line broadening of NH resonances and the observation of medium range NH(i)<-> NH(i+2) NOEs established the presence of conformational heterogeneity for the tetrapeptide in CDCl3 solution. The NMR results are consistent with the limited population of the continuous C-12 helix conformation. Lengthening of the (alpha gamma)(n) sequences in the nonapeptides Boc-Aib-Gpn-Aib-Gpn-Aib-Gpn-Aib-Gpn-Xxx (Xxx = Aib, Leu) resulted in the observation of all of the sequential NOEs characteristic of an alpha gamma C-12 helix. These results establish that conformational fragility is manifested in short hybrid alpha gamma sequences despite the choice of conformationally constrained residues, while stable helices are formed on chain extension.