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.
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