Role of non-planar peptide unit in regular polypeptide helices. New model for poly-beta-benzyl-L-Aspartate

Int J Pept Protein Res. 1981 Oct;18(4):374-82. doi: 10.1111/j.1399-3011.1981.tb02995.x.


The effect of non-planarity of the peptide unit on helical structures stabilized by intrachain hydrogen bonds is discussed. While the present calculations generally agree with those already reported in the literature for right-handed helical structures, it is found that the most stable left-handed structure is a novel helix, called the delta-helix. Its helical parameters are close to these reported for poly-beta-benzyl-L -aspartate. Conformational energy calculations show that poly-beta-benzyl-L -aspartate with the delta-helical structure is considerably more stable than the structure it is generally believed to take up (the omega-helix) by about 15 kcal/mol-residue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Hydrogen Bonding
  • Macromolecular Substances
  • Models, Chemical*
  • Peptides*
  • Protein Conformation


  • Macromolecular Substances
  • Peptides
  • poly-beta-benzyl-aspartate