1l2y
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(New page: 200px<br /> <applet load="1l2y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2y" /> '''NMR Structure of Trp-Cage Miniprotein Const...)
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Revision as of 06:56, 18 November 2007
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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
1L2Y is a Protein complex structure of sequences from [1]. 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
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