De novo design: backbone conformational constraints in nucleating helices andβ-hairpins

Authors

  • P. Balaram

    1. Molecular Biophysics Unit, Indian Institute of Science and Chemical Biology Unit, Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore 560012, India.
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  • To cite this article:

    Balaram, P. De novo design: backbone conformational constraints in nucleating helices and b-hairpins.

    J. Peptide Res., 1999, 54, 195–199


Professor P. Balaram
Molecular Biophysics Unit
Indian Institute of Science
Bangalore 560 012
India
Fax: 91-80-334-1683/91-80-334-8535
E-mail:pb@mbu.iisc.ernet.in

Abstract

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.

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