The Structure of the Polycyclic Nonadecapeptide Ro 09‐0198

Horst Kessler; Stefan Steuernagel; Martin Will; Günther Jung; Roland Kellner; Dieter Gillessen; Tsutomu Kamiyama

doi:10.1002/hlca.19880710811

The Structure of the Polycyclic Nonadecapeptide Ro 09‐0198

Horst Kessler
, Stefan Steuernagel
, Martin Will
, Günther Jung
, Roland Kellner
, Dieter Gillessen
, Tsutomu Kamiyama

Johann Wolfgang Goethe University
University of Tübingen
Roche Pharma Research & Early Development
Nippon Roche Research Center

Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

51 Zitate (Scopus)

Abstract

The conventional determination of the amino‐acid sequence of the peptide antibiotic Ro 09‐0198 was prevented by four cyclizations via side chains. The joint application of NMR spectroscopy at highest field and automated Edman degradation yielded a complete determination of the connectivity pattern. The three‐dimensional structure derived from NOE data exhibits an interesting separation of amino acids with hydrophilic and hydrophobic side chains.

Originalsprache	Englisch
Seiten (von - bis)	1924-1929
Seitenumfang	6
Fachzeitschrift	Helvetica Chimica Acta
Jahrgang	71
Ausgabenummer	8
DOIs	https://doi.org/10.1002/hlca.19880710811
Publikationsstatus	Veröffentlicht - 14 Dez. 1988
Extern publiziert	Ja

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abstract = "The conventional determination of the amino‐acid sequence of the peptide antibiotic Ro 09‐0198 was prevented by four cyclizations via side chains. The joint application of NMR spectroscopy at highest field and automated Edman degradation yielded a complete determination of the connectivity pattern. The three‐dimensional structure derived from NOE data exhibits an interesting separation of amino acids with hydrophilic and hydrophobic side chains.",

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AU - Jung, Günther

AU - Kellner, Roland

AU - Gillessen, Dieter

AU - Kamiyama, Tsutomu

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AB - The conventional determination of the amino‐acid sequence of the peptide antibiotic Ro 09‐0198 was prevented by four cyclizations via side chains. The joint application of NMR spectroscopy at highest field and automated Edman degradation yielded a complete determination of the connectivity pattern. The three‐dimensional structure derived from NOE data exhibits an interesting separation of amino acids with hydrophilic and hydrophobic side chains.

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DO - 10.1002/hlca.19880710811

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The Structure of the Polycyclic Nonadecapeptide Ro 09‐0198

Abstract

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