Protein design as a challenge for peptide chemists

A review with 37 refs. In the present review, various attempts to apply synthetic tools for inducing native-like structural features in peptides in order to bypass the folding problem are described. Besides well-established methods for the nucleation and stabilization of secondary structures, e.g. a-helixes, b-sheets and b-turns, topol. templates as 'built-in' folding devices have more recently become the key elements for the induction of protein-like folding units (template-assembled synthetic proteins, TASP). Progress in the synthetic strategy and structural characterization of this new type of macromols. opens the way for the design of functional TASP mols. [on SciFinder (R)]

Published in:
Journal of Peptide Science, 1, Launch Issue, 3-10

 Record created 2006-02-09, last modified 2018-01-27

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