Ramachandran, GN and Chandrasekharan, R and Chidambaram, R (1971) Potential functions for hydrogen bond interactions - IV. Minimum Energy Conformation of the α-Helical Structure of PoIy-L-Alanine. In: Proceedings of the Indian Academy of Sciences - Section A, 74 (6). pp. 284-298.
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Abstract
Making use of the empirical potential functions for peptide NH .. O bonds, developed in this laboratory, the relative stabilities of the rightand left-handed α-helical structures of poly-L-alanine have been investigated, by calculating their conformational energies (V). The value of Vmin of the right-handed helix (αP) is about - 10.4 kcal/mole, and that of the left-handed helix (αM) is about - 9.6 kcal/mole, showing that the former is lower in energy by 0.8 kcal/mole. The helical parameters of the stable conformation of αP are n ∼ 3.6 and h ∼ 1.5 Å. The hydrogen bond of length 2.85 Å and nonlinearity of about 10° adds about 4.0 kcal/ mole to the stabilising energy of the helix in the minimum enregy region. The energy minimum is not sharply defined, but occurs over a long valley, suggesting that a distribution of conformations (φ{symbol}, ψ) of nearly the same energy may occur for the individual residues in a helix. The experimental data of a-helical fibres of poly-L-alanine are in good agreement with the theoretical results for αP. In the case of proteins, the mean values of (φ{symbol}, ψ) for different helices are distributed, but they invariably occur within the contour for V = Vmin + 2 kcal/mole for αP.
Item Type: | Journal Article |
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Publication: | Proceedings of the Indian Academy of Sciences - Section A |
Publisher: | Indian Academy of Sciences |
Additional Information: | Copyright of this article belongs to Indian Academy of Sciences. |
Department/Centre: | Division of Physical & Mathematical Sciences > Physics |
Date Deposited: | 11 Jun 2010 08:18 |
Last Modified: | 25 Oct 2018 09:19 |
URI: | http://eprints.iisc.ac.in/id/eprint/28330 |
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