To cite this article:
De novo design: backbone conformational constraints in nucleating helices andβ-hairpins
Article first published online: 9 OCT 2008
The Journal of Peptide Research
Volume 54, Issue 3, pages 195–199, September 1999
How to Cite
Balaram, P. (1999), De novo design: backbone conformational constraints in nucleating helices andβ-hairpins . The Journal of Peptide Research, 54: 195–199. doi: 10.1034/j.1399-3011.1999.00119.x
Balaram, P. De novo design: backbone conformational constraints in nucleating helices and b-hairpins.
J. Peptide Res., 1999, 54, 195–199
- Issue published online: 9 OCT 2008
- Article first published online: 9 OCT 2008
- Dates:Received 26 October 1998Revised 25 March 1999Accepted 4 May 1999
- de novo design ;
- peptide design
Abstract: A modular approach to synthetic protein design is being developed using conformationally constrained amino acid as stereochemical directors of polypeptide chain folding. An overview of studies aimed at constructing peptide helices using α,α-dialkyated residues and β-hairpins using d-Pro as a turn nucleator is presented. The construction of helix-helix motifs and three- and four-stranded structures has been achieved using non-protein amino acids to stabilize specific elements of secondary structures.