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Conformational aspects of polypeptides. XXIV. Conformational energies of poly-N-methyl-L-alanine chains

✍ Scribed by J. E. Mark; Murray Goodman

Publisher: Wiley (John Wiley & Sons)
Year: 1967
Tongue: English
Weight: 324 KB
Volume: 5
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.1967.360050903

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✦ Synopsis

Conformational energies of the poly-N-methyl-halanine chain have been calculated as a function of the rotational angles of its skeletal bonds, taking into account torsional potentials, van der Waals repulsions, and London attractions. Four pronounced minima in the energy were found; the relative magnitudes of the energies at these minima suggest that the preferred conformation of this chain is either a right-handed, approximately threefold helix, or a slightly distorted, left-handed a-helix. Inclusion of an estimate of the dipolar contribution to the total conformational energy does not significantly affect this conclusion.

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