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Issue 20, 2003
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Novel conformationally-constrained β-peptides characterized by 1H NMR chemical shifts

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Abstract

For a novel family of oxanorbornene β-peptides, density functional theory computations of the three-dimensional structure and 1H NMR chemical shifts predict that the dimer and trimer form consecutive 8-membered hydrogen-bonded ring helices, which is supported by excellent agreement with experimental solution NMR data.

Graphical abstract: Novel conformationally-constrained β-peptides characterized by 1H NMR chemical shifts

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Publication details

The article was received on 11 Aug 2003, accepted on 11 Sep 2003 and first published on 23 Sep 2003


Article type: Communication
DOI: 10.1039/B309584C
Citation: Chem. Commun., 2003,0, 2534-2535
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    Novel conformationally-constrained β-peptides characterized by 1H NMR chemical shifts

    R. J. Doerksen, B. Chen, J. Yuan, J. D. Winkler and M. L. Klein, Chem. Commun., 2003, 0, 2534
    DOI: 10.1039/B309584C

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