1l2y

NMR Structure of Trp-Cage Miniprotein Construct TC5b

spinqualitylabelsall models 1l2y Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1l2y is a 1 chain structure. The October 2005 RCSB PDB Molecule of the Month feature on Designer Proteins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_10. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Designing a 20-residue protein.,Neidigh JW, Fesinmeyer RM, Andersen NH Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:11979279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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