ISSN:
0006-3525
Keywords:
Poly(β-L-aspartate)s
;
helical conformations
;
quantum mechanical calculations
;
cooperative energy effects
;
helix stability
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformational preferences of the monomeric units of a series of poly(α-alkyl-β-L-aspartate)s were examined by quantum mechanical calculations. α-Alkyl-β-aspartamyl m-oligopeptides with a number of residues m ranging from 1 to 7 and arranged in the conformations experimentally observed for their corresponding polymers were computed. Both their total relative energies and their cooperative energy differences were compared as a function of the length of the oligopeptide and the nature of the alkyl side group. Results revealed that the 13/4 helical arrangement is the most stable structure for the isolated polymer chain for any side group, although a 17/4 helix becomes favored in the case of methyl and ethyl groups due to the packing effects. On the other hand, the stability of the 4/1 helix appears to be the preferred conformation for side groups with a branched constitution. © 1997 John Wiley & Sons, Inc. Biopoly 41: 721-729, 1997
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
