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Issue 11, 2003
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Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from Cα-methyl-leucine

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Abstract

A series of [L-(αMe)Leu]n (n = 1–5) homo-peptides have been covalently linked to Tentagel and POEPOP resins and submitted to a conformational study using HRMAS NMR spectroscopy. Whereas the mono- and dipeptide are mainly fully-extended, stable 310-helical structures are formed beginning from the trimer.

Graphical abstract: Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from Cα-methyl-leucine

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Publication details

The article was received on 24 Mar 2003, accepted on 01 May 2003 and first published on 02 May 2003


Article type: Communication
DOI: 10.1039/B303193D
Citation: Org. Biomol. Chem., 2003,1, 1835-1837
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    Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from Cα-methyl-leucine

    M. Rainaldi, N. Lancelot, K. Elbayed, J. Raya, M. Piotto, J. Briand, B. Kaptein, Q. B. Broxterman, A. Berkessel, F. Formaggio, C. Toniolo and A. Bianco, Org. Biomol. Chem., 2003, 1, 1835
    DOI: 10.1039/B303193D

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