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| | {{STRUCTURE_2evq| PDB=2evq | SCENE= }} | | {{STRUCTURE_2evq| PDB=2evq | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16669679}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16669679 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16669679}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVQ OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVQ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Peptide]] | | [[Category: Peptide]] |
| | [[Category: Trp/trp packing]] | | [[Category: Trp/trp packing]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:10:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:33:41 2008'' |
Revision as of 06:33, 29 July 2008
Template:STRUCTURE 2evq
Solution structure of HP7, a 12-residue beta hairpin
Template:ABSTRACT PUBMED 16669679
About this Structure
Full experimental 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 Tue Jul 29 09:33:41 2008
