1l2y: Difference between revisions
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'''NMR Structure of Trp-Cage Miniprotein Construct TC5b''' | {{Structure | ||
|PDB= 1l2y |SIZE=350|CAPTION= <scene name='initialview01'>1l2y</scene> | |||
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'''NMR Structure of Trp-Cage Miniprotein Construct TC5b''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L2Y is a [ | 1L2Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1L2Y with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Y OCA]. | ||
==Reference== | ==Reference== | ||
Designing a 20-residue protein., Neidigh JW, Fesinmeyer RM, Andersen NH, Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:[http:// | Designing a 20-residue protein., Neidigh JW, Fesinmeyer RM, Andersen NH, Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11979279 11979279] | ||
[[Category: Designer Proteins]] | [[Category: Designer Proteins]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: two-state folding]] | [[Category: two-state folding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:35 2008'' | ||
Revision as of 10:25, 20 March 2008
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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
Page seeded by OCA on Thu Mar 20 12:25:35 2008
