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1l2y
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jrj|1jrj]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2y OCA], [http://www.ebi.ac.uk/pdbsum/1l2y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l2y RCSB]</span> | ||
}} | }} | ||
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[[Category: two-state folding]] | [[Category: two-state folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:57:13 2008'' |
Revision as of 18:57, 30 March 2008
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| Related: | 1jrj
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Sun Mar 30 21:57:13 2008
