Karle, I. L. ; Flippen-Anderson, J. L. ; Uma, K. ; Balaram, P. (1990) Helix construction using α-aminoisobutyryl residues in a modular approach to synthetic protein design. Conformational properties of an apolar decapeptide in two different crystal forms and in solution Current Science, 59 (17-18). pp. 875-885. ISSN 0011-3891
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Abstract
A modular strategy for the assembly of synthetic protein mimics is outlined. This approach is based on the ability of α -aminoisobutyric acid (Aib) to promote helical folding in peptides. The design of apolar, peptide helices with a high solubility in organic solvents facilitates structural design based on stereochemical constraints imposed by chosen non-protein residues. The design of individual helices is illustrated by the analysis of the decapeptide Boc-Aib-Ala-Leu-A!a-Aib-Aib-Leu-~Ala-Leu-Aib-OMe. Crystal structures of two polymorphic forms reveal an almost completely α-helical backbone. These high-resolution structures permit detailed characterization of the helix. H NMR and CD studies demonstrate maintenance of the helical conformation in solution, a feature that is a consequence of the limited flexibility of Aib residues in φ, ψ space.
Item Type: | Article |
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Source: | Copyright of this article belongs to Current Science Association. |
ID Code: | 91394 |
Deposited On: | 21 May 2012 08:41 |
Last Modified: | 19 May 2016 05:13 |
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