Parallel Sheet Secondary Structure in β-Peptides

Authors

  • Joseph M. Langenhan,

    1. Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, WI 53706, USA, Fax: (+1) 608-265-4534
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  • Ilia A. Guzei Dr.,

    1. Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, WI 53706, USA, Fax: (+1) 608-265-4534
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    • Correspondence regarding X-ray diffraction analysis should be addressed to I.A.G. (E-mail: iguzei@chem.wisc.edu).

  • Samuel H. Gellman Prof.

    1. Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, WI 53706, USA, Fax: (+1) 608-265-4534
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  • This research was supported by the U.S. National Institutes of Health (GM 56414). J.M.L. was supported in part by a National Science Foundation Predoctoral Fellowship. The NMR spectrometer was purchased in part with a U.S. National Institutes of Health grant (NIH 1 S10 RR13866-01).

Abstract

original image

Diamin-verbrücktesyn-α,β-Dialkyl-β-aminosäureeinheiten (siehe Bild) bilden parallele Faltblatt-Sekundärstrukturen. Die Konfiguration der verbrückenden Gruppe beeinflusst die Bildung der parallelen Haarnadel-Struktureinheiten in diesem Fall in geringerem Maße als bei analogen α-Peptidsystemen.

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