De novo design: backbone conformational constraints in nucleating helices and beta-hairpins.
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 alpha,alpha-dialkyated residues and beta-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.
Balaram
P
P
Molecular Biophysics Unit, Indian Institute of Science and Chemical Biology Unit, Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore. pb@mbu.iisc.ernet.in
D000596:Amino Acids / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry
D000596:Amino Acids; D010455:Peptides; D011506:Proteins