1l2y: Difference between revisions

[[Image:1l2y.gif|left|200px]]<br /><applet load="1l2y" size="350" color="white" frame="true" align="right" spinBox="true"  

Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are &gt;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.

1L2Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1L2Y with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Y OCA].  

[[Category: Andersen, N H.]]

[[Category: Fesinmeyer, R M.]]

[[Category: Neidigh, J W.]]

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