Bansal, Manju and Brahmachari, Samir K and Sasisekharan, V (1979) Structural Investigations on Poly(4-hydroxy-L-proline). 1. Theoretical Studies. In: Macromolecules, 12 (1). pp. 19-23.
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Model building studies on poly(hydroxypro1ine) indicate that in addition to the well-known helical structure of form A, a left-handed helical structure with trans peptide units and with h = 2.86 A and n = 2.67 (i.e., 8 residues in 3 turns) is also possible. In this structure which is shown to be in agreement with X-ray data of the form B in the next paper, the y-hydroxyl group of an (i + 1)th Hyp residue is hydrogen bonded to the carbonyl oxygen of an (i - 1)th residue. The possibility of a structure with cis peptide units is ruled out. It is shown that both forms A and B are equally favorable from considerations of intramolecular energies. Since form B is further stabilized by intrachain hydrogen bonds, we believe that this is likely to be the ordered conformation for poly(hydroxypro1ine) in water.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to American Chemical Society.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||27 Dec 2010 11:58|
|Last Modified:||27 Dec 2010 11:58|
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