Designing a 20-residue protein
Top Cited Papers
- 29 April 2002
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 9 (6), 425-430
- https://doi.org/10.1038/nsb798
Abstract
Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are >95% folded in water at physiological pH. These constructs optimize a novel fold, designated as the 'Trp-cage' motif, and are significantly more stable than any other miniprotein reported to date. Folding is cooperative and hydrophobically driven by the encapsulation of a Trp side chain in a sheath of Pro rings. As the smallest protein-like construct, Trp-cage miniproteins should provide a testing ground for both experimental studies and computational simulations of protein folding and unfolding pathways. Pro–Trp interactions may be a particularly effective strategy for the a priori design of self-folding peptides.Keywords
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