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2evq

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[[Image:2evq.gif|left|200px]]
[[Image:2evq.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2evq", creates the "Structure Box" on the page.
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{{STRUCTURE_2evq| PDB=2evq | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2evq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2evq OCA], [http://www.ebi.ac.uk/pdbsum/2evq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2evq RCSB]</span>
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'''Solution structure of HP7, a 12-residue beta hairpin'''
'''Solution structure of HP7, a 12-residue beta hairpin'''
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==About this Structure==
==About this Structure==
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2EVQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVQ OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVQ OCA].
==Reference==
==Reference==
Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16669679 16669679]
Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16669679 16669679]
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[[Category: Protein complex]]
 
[[Category: Andersen, N H.]]
[[Category: Andersen, N H.]]
[[Category: Fesinmeyer, R M.]]
[[Category: Fesinmeyer, R M.]]
[[Category: Olsen, K A.]]
[[Category: Olsen, K A.]]
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[[Category: beta hairpin]]
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[[Category: Beta hairpin]]
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[[Category: peptide]]
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[[Category: Peptide]]
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[[Category: trp/trp packing]]
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[[Category: Trp/trp packing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:10:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:54:25 2008''
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Revision as of 00:10, 4 May 2008

Template:STRUCTURE 2evq

Solution structure of HP7, a 12-residue beta hairpin


Overview

Minimized beta hairpins have provided additional data on the geometric preferences of Trp interactions in TW-loop-WT motifs. This motif imparts significant fold stability to peptides as short as 8 residues. High-resolution NMR structures of a 16- (KKWTWNPATGKWTWQE, DeltaG(U)(298) >or= +7 kJ/mol) and 12-residue (KTWNPATGKWTE, DeltaG(U)(298) = +5.05 kJ/mol) hairpin reveal a common turn geometry and edge-to-face (EtF) packing motif and a cation-pi interaction between Lys(1) and the Trp residue nearest the C-terminus. The magnitude of a CD exciton couplet (due to the two Trp residues) and the chemical shifts of a Trp Hepsilon3 site (shifted upfield by 2.4 ppm due to the EtF stacking geometry) provided near-identical measures of folding. CD melts of representative peptides with the -TW-loop-WT- motif provided the thermodynamic parameters for folding, which reflect enthalpically driven folding at laboratory temperatures with a small DeltaC(p) for unfolding (+420 J K(-)(1)/mol). In the case of Asx-Pro-Xaa-Thr-Gly-Xaa loops, mutations established that the two most important residues in this class of direction-reversing loops are Asx and Gly: mutation to alanine is destabilizing by about 6 and 2 kJ/mol, respectively. All indicators of structuring are retained in a minimized 8-residue construct (Ac-WNPATGKW-NH(2)) with the fold stability reduced to DeltaG(U)(278) = -0.7 kJ/mol. NMR and CD comparisons indicate that -TWXNGKWT- (X = S, I) sequences also form the same hairpin-stabilizing W/W interaction.

About this Structure

Full crystallographic information is available from OCA.

Reference

Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:16669679 Page seeded by OCA on Sun May 4 03:10:00 2008

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