This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1l2y
From Proteopedia
NMR Structure of Trp-Cage Miniprotein Construct TC5b
Overview
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.
About this Structure
The following page contains interesting information on the relation of 1L2Y with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
Designing a 20-residue protein., Neidigh JW, Fesinmeyer RM, Andersen NH, Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:11979279 Page seeded by OCA on Fri May 2 23:28:53 2008
