Výsledky vyhledávání

Akademický článek

Long Polypeptide 310-helices at Atomic Resolution

Autor: Bavoso, Alfonso, Benedetti, Ettore, Di Blasio, Benedetto, Pavone, Vincenzo, Pedone, Carlo, Toniolo, Claudio, Bonora, Gian Maria

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 1986 Apr 01. 83(7), 1988-1992.

Externí odkaz: https://www.jstor.org/stable/27123

Zobrazit plný text záznamu

Accommodation of aD-Phe residue into a right-handed 310-helix: Structure of Boc-D-Phe-(Aib)4-Gly-L-Leu-(Aib)2-Ome, an analogue of the amino terminal segment of antiamoebins and emerimicins

Autor: Padmanabhan Balaram, Judith L. Flippen-Anderson, Isabella L. Karle, K. Uma

Publikováno v: Biopolymers. 33:401-407

The crystal structure of the nonapeptide Boc-D-Phe-Aib-Aib-Aib-Aib-Gly-Leu-Aib-Aib-OMe (I), which is an analogue of the N-terminal sequence of antiamoebins and emerimicins, establishes a completely 3(10)-helical conformation with seven successive int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9a86219fd0496f2053e985178d89113
https://doi.org/10.1002/bip.360330308

Zobrazit plný text záznamu

ChemInform Abstract: Emerimicins III and IV and Their Ethylalanine12 Epimers. Facilitated Chemical-Enzymatic Synthesis and a Qualitative Evaluation of Their Solution Structures

Autor: William C. Hutton, Karol Kociolek, Miroslaw T. Leplawy, Fritz Reusser, Janusz Zabrocki, Denise D. Beusen, Urszula Slomczynska, Adam S. Redlinski, Garland R. Marshall

Publikováno v: ChemInform. 23

The peptaibol antibiotics, emerimicin III and IV (Ac-Phe 1 -MeA 2 -MeA 3 -MeA 4 -Val 5 -Gly 6 -Leu 7 -MeA 8 -MeA 9 - Hyp 10 -Gln 11 -R-EtA 12 -Hyp 13 -Xxx 14 -Phol 15 , where Xxx=Ala for emerimicin III and Xxx=MeA for emerimicin IV) and their EtA 12

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1e1be66894ccf533957d368e460dd89a
https://doi.org/10.1002/chin.199237282

Zobrazit plný text záznamu

Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures

Autor: William C. Hutton, Karol Kociolek, Denise D. Beusen, Urszula Slomczynska, Janusz Zabrocki, Garland R. Marshall, Adam S. Redlinski, Fritz Reusser, Miroslaw T. Leplawy

Publikováno v: Journal of the American Chemical Society. 114:4095-4106

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e243db448525a62595aaa04fac9f8e90
https://doi.org/10.1021/ja00037a010

Zobrazit plný text záznamu

Linear oligopeptides: peptaibol antibiotics — preferred conformation of the 2–9 segment of emerimicins III and IV and all related short sequences

Autor: Carlo Pedone, Gian Maria Bonora, Benedetto Di Blasio, Alfonso Bavoso, Claudio Toniolo, Ettore Benedetti, Vincenzo Pavone

Publikováno v: International Journal of Biological Macromolecules. 7:357-362

With the aim of obtaining information on the effect induced by main-chain length and amino acid sequence on the type of helical structure adopted by naturally-occurring peptides rich in Cα,α-dialkylated residues, an infrared absorption and 1H nucle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba5758d2a9b0ff52aa63a7467dfdd823
https://doi.org/10.1016/0141-8130(85)90050-9

Zobrazit plný text záznamu

Peptaibol antibiotics: Conformational preferences of synthetic emerimicin fragments

Autor: Carlo Pedone, Gian Maria Bonora, Vincenzo Pavone, Claudio Toniolo, Benedetto Di Blasio, Alfonso Bavoso, Ettore Benedetti

Publikováno v: Biopolymers. 22:1335-1356

The ir absorption and CD conformational analyses of solutions of the protected 2–9 fragment of the peptaibol antibiotics emerimicins III and IV and related short sequences are consistent with the presence of a right-handed α-helix for the octapept

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f1d7b2abe8676a46e689585ceafe3a95
https://doi.org/10.1002/bip.360220507

Zobrazit plný text záznamu

Molecular Structure of Peptaibol Antibiotics: Solution Conformation and Crystal Structure of the Octapeptide Corresponding to the 2–9 Sequence of Emerimicins III and IV

Autor: Carlo Pedone, Vincenzo Pavone, Alfonso Bavoso, Gian Maria Bonora, Claudio Toniolo, Benedetto di Biasio, Ettore Benedetti

Publikováno v: Journal of Biomolecular Structure and Dynamics. 3:585-598

The infrared absorption and 1H nuclear magnetic resonance analyses of chloroform solutions of the terminally-blocked segment corresponding to the 2-9 sequence of emerimicins III and IV, -(Aib)3-L-Val-Gly-L-Leu-(Aib)2-, are consistent with the presenc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62afe9509de59c100e2acc7f213aabb9
https://doi.org/10.1080/07391102.1985.10508446

Zobrazit plný text záznamu

Peptaibol antibiotics: a study on the helical structure of the 2-9 sequence of emerimicins III and IV

Autor: Carlo Pedone, Claudio Toniolo, Alfonso Bavoso, B. Di Blasio, Vincenzo Pavone, Ettore Benedetti, Gian Maria Bonora

Publikováno v: Proceedings of the National Academy of Sciences. 79:7951-7954

Solution conformations of the protected 2-9 segment of the peptaibol antibiotics emerimicins III and IV [alpha-aminoisobutyric acid (Aib)]3-L-Val-Gly-L-Leu-(Aib)2 and the related short sequences benzyloxy-(Aib)3-L-Val-OMe and benzyloxy-(Aib)3-L-Val-G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c123ee8d50694bbba8c3decd4f64a4c
https://doi.org/10.1073/pnas.79.24.7951

Zobrazit plný text záznamu

Akademický článek

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

Vyhledávací nástroje:

Upřesnit hledání