1l2y: Difference between revisions
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'''NMR Structure of Trp-Cage Miniprotein Construct TC5b''' | '''NMR Structure of Trp-Cage Miniprotein Construct TC5b''' | ||
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==About this Structure== | ==About this Structure== | ||
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://www.ncbi.nlm.nih.gov/pubmed/11979279 11979279] | 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: Andersen, N H.]] | [[Category: Andersen, N H.]] | ||
[[Category: Fesinmeyer, R M.]] | [[Category: Fesinmeyer, R M.]] | ||
[[Category: Neidigh, J W.]] | [[Category: Neidigh, J W.]] | ||
[[Category: | [[Category: Miniprotein]] | ||
[[Category: | [[Category: Trp-cage]] | ||
[[Category: | [[Category: Two-state folding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:28:53 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:28, 2 May 2008
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
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 Fri May 2 23:28:53 2008
