Balaram, P. (1999) De novo design: backbone conformational constraints in nucleating helices and β-hairpins The Journal of Peptide Research, 54 (3). pp. 195-199. ISSN 1397-002X
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Official URL: http://www3.interscience.wiley.com/journal/1214459...
Related URL: http://dx.doi.org/10.1034/j.1399-3011.1999.00119.x
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons, Inc. |
Keywords: | De Novo Design; Helices; β-hairpins; Peptide Design |
ID Code: | 4445 |
Deposited On: | 18 Oct 2010 07:51 |
Last Modified: | 16 May 2016 15:06 |
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