Critical Main-Chain Length for Conformational Conversion From 310-Helix to α-Helix in Polypeptides
- 1 June 1990
- journal article
- research article
- Published by Taylor & Francis in Journal of Biomolecular Structure and Dynamics
- Vol. 7 (6) , 1321-1331
- https://doi.org/10.1080/07391102.1990.10508568
Abstract
To assess the minimal peptide length required for the stabilization of the a-helix relative to the 310-helix in Aib-rich peptides, we have solved the X-ray diffraction structures of the terminally blocked sequential hexa- and octapeptides with the general formula -(Aib-L-Ala)n-(n = 3 and 4, respectively). The hexapeptide molecules are completely 310-helical with four 1 ← 4 intramolecular N-H … O=C H-bonds. On the other hand, the octapeptide molecules are essentially α-helical with four 1 ← 5 H-bonds; however, the helix is elongated at the N-terminus, with two 1 ← 4 H-bonds, giving these molecules a mixed α/310-helical character. In both compounds the right-handed screw sense of the helix is dictated by the presence of the Ala residues of L-configuration. This study represents the first experimental proof for a 310 →α-helix conversion in the crystal state induced by peptide backbone lengthening only.This publication has 27 references indexed in Scilit:
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