Sasisekharan, V and Balaji, VN (1979) Fourfold Helical Structures for Polypeptides. In: Macromolecules, 12 (1). 28-32 .
Helical.pdf - Published Version
Restricted to Registered users only
Download (626Kb) | Request a copy
Fourfold helical structures for polypeptides and their association in regular lattices with interchain hydrogen bonds were investigated by model building studies. These studies revealed that stereochemically satisfactory fourfold helical sturctures are possible for polyglycine, polyproline, and copolymers of glycine and proline with two and four units in the monomer. In these structures the unit height h for the backbone has been found to be restricted from 2.7 to 3.1 k, with four peptide units per turn of the helix. Energetically both fourfold and threefold helical structures are equally favorable.
|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:||22 Dec 2010 11:34|
|Last Modified:||22 Dec 2010 11:34|
Actions (login required)