1l2y
From Proteopedia
(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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'''NMR Structure of Trp-Cage Miniprotein Construct TC5b'''<br /> | '''NMR Structure of Trp-Cage Miniprotein Construct TC5b'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Truncation and mutation of a poorly folded 39-residue peptide has produced | + | 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== | ==About this Structure== | ||
| - | 1L2Y is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | + | 1L2Y is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Designer Proteins]] | [[Category: Designer Proteins]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Andersen, N | + | [[Category: Andersen, N H.]] |
| - | [[Category: Fesinmeyer, R | + | [[Category: Fesinmeyer, R M.]] |
| - | [[Category: Neidigh, J | + | [[Category: Neidigh, J W.]] |
[[Category: miniprotein]] | [[Category: miniprotein]] | ||
[[Category: trp-cage]] | [[Category: trp-cage]] | ||
[[Category: two-state folding]] | [[Category: two-state folding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:44 2008'' |
Revision as of 11:40, 21 February 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 Feb 21 13:40:44 2008
