From Proteopedia
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| - | [[Image:2dx3.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2dx3| PDB=2dx3 | SCENE= }} | | {{STRUCTURE_2dx3| PDB=2dx3 | SCENE= }} |
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| - | '''NMR structure of DP5_conformation1: monomeric alpha-helix'''
| + | ===NMR structure of DP5_conformation1: monomeric alpha-helix=== |
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| - | ==Overview==
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| - | Intrinsic rules of determining the tertiary structure of a protein have been unknown partly because physicochemical factors that contribute to stabilization of a protein structure cannot be represented as a linear combination of local interactions. To clarify the rules on the nonlinear term caused by nonlocal interaction in a protein, we tried to transform a peptide that has a fully helical structure (Target Peptide or TP) into a peptide that has a beta-hairpin structure (Designed Peptide or DP) by adding seven residues to the C terminus of TP. According to analyses of nuclear magnetic resonance measurements, while the beta-hairpin structure is stabilized in some DPs, it is evident that the helical structure observed in TP is also persistent and even extended throughout the length of the molecule. As a result, we have produced a peptide molecule that contains both the alpha-helix and beta-hairpin conformation at an almost equally populated level. The helical structures contained in these DPs were more stable than the helix in TP, suggesting that stabilizing one conformation does not result in destabilizing the other conformation. These DPs can thus be regarded as an isolated peptide version of the chameleon sequence, which has the capability of changing the secondary structure depending on the context of the surrounding environment in a protein structure. The fact that the transformation of one secondary structure caused stabilization of both the original and the induced structure would shed light on the mechanism of protein folding.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17177204}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17177204 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17177204}} |
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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=2DX3 OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DX3 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Tamura, A.]] | | [[Category: Tamura, A.]] |
| | [[Category: Alpha-helix]] | | [[Category: Alpha-helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:33:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:05:07 2008'' |
Revision as of 06:05, 28 July 2008
Template:STRUCTURE 2dx3
NMR structure of DP5_conformation1: monomeric alpha-helix
Template:ABSTRACT PUBMED 17177204
About this Structure
Full experimental information is available from OCA.
Reference
Transformation of an alpha-helix peptide into a beta-hairpin induced by addition of a fragment results in creation of a coexisting state., Araki M, Tamura A, Proteins. 2007 Mar 1;66(4):860-8. PMID:17177204
Page seeded by OCA on Mon Jul 28 09:05:07 2008
