1L2Y

NMR Structure of Trp-Cage Miniprotein Construct TC5b

Summary for 1L2Y

Entry DOI	10.2210/pdb1l2y/pdb
Related	1jrj
NMR Information	BMRB: 5292
Descriptor	TC5b (1 entity in total)
Functional Keywords	miniprotein, two-state folding, trp-cage, de novo protein
Total number of polymer chains	1
Total formula weight	2171.41
Authors	Neidigh, J.W.,Fesinmeyer, R.M.,Andersen, N.H. (deposition date: 2002-02-25, release date: 2002-05-29, Last modification date: 2024-05-08)
Primary citation	Neidigh, J.W.,Fesinmeyer, R.M.,Andersen, N.H. Designing a 20-residue protein. Nat.Struct.Biol., 9:425-430, 2002 Cited by PubMed 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. PubMed: 11979279 DOI: 10.1038/nsb798 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation