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   <subfield code="a">Complete1H- and13C-NMR spectroscopic assignment of two pentadecapeptides by reverse C,H correlation techniques</subfield>
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   <subfield code="c">[Hermann Kalchhauser, Martin Kriech, Horst Ahorn, W. Sommergruber]</subfield>
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   <subfield code="a">Vollständige1H- und13C-NMR-spektroskopische Zuordnung von zwei Pentadecapeptiden mittels invers detektierter C,H-Korrelationstechniken</subfield>
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   <subfield code="a">Summary: Two oligopeptides representing a wild type and a modified version of the polyprotein cleavage region for proteinase2 A of the human rhinovirus type 2 (HRV 22 A) have been investigated using homo- and heterocorrelated 2 D NMR spectroscopy. Proton-detected C,H correlation techniques turned out to be extremely useful for sequential resonance assignment. In one case, the complete amino acid backbone could be analyzed without using NOESY spectra, thus avoiding ambiguities inherent to this method. No defined tertiary structure of the cleavage region could be detected in either molecule. However, one of the oligopeptides is present to a very low extent in a conformation different from therandom-coil arrangement.</subfield>
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