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| - | [[Image:2jm0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2jm0.png|left|200px]] |
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| | {{STRUCTURE_2jm0| PDB=2jm0 | SCENE= }} | | {{STRUCTURE_2jm0| PDB=2jm0 | SCENE= }} |
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| - | '''Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core'''
| + | ===Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core=== |
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| - | ==Overview==
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| - | We report the first high-resolution structure for a protein containing a fluorinated side chain. Recently we carried out a systematic evaluation of phenylalanine to pentafluorophenylalanine (Phe --> F(5)-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe --> F(5)-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than either aryl-aryl or perfluoroaryl-perfluoroaryl interactions, and because perfluoroaryl units are more hydrophobic than are analogous aryl units. Only one mutation, Phe10 --> F(5)-Phe, was found to provide enhanced tertiary structural stability relative to the native core (by approximately 1 kcal/mol, according to guanidinium chloride denaturation studies). The NMR structure of this mutant, described here, reveals very little variation in backbone conformation or side chain packing relative to the wild type. Thus, although Phe --> F(5)-Phe mutations offer the possibility of greater tertiary structural stability from side chain-side chain attraction and/or side chain desolvation, the constraints associated with the native c-VHP fold apparently prevent the modified polypeptide from taking advantage of this possibility. Our findings are important because they complement several studies that have shown that fluorination of saturated side chain carbon atoms can provide enhanced conformational stability.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17123960}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17123960 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17123960}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2JM0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM0 OCA]. | + | 2JM0 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM0 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Fluorinated phe]] | | [[Category: Fluorinated phe]] |
| | [[Category: Vhp]] | | [[Category: Vhp]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:00:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:55:24 2008'' |
Revision as of 18:55, 27 July 2008
Template:STRUCTURE 2jm0
Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core
Template:ABSTRACT PUBMED 17123960
About this Structure
2JM0 is a Single protein structure. Full experimental information is available from OCA.
Reference
Solution structure of a small protein containing a fluorinated side chain in the core., Cornilescu G, Hadley EB, Woll MG, Markley JL, Gellman SH, Cornilescu CC, Protein Sci. 2007 Jan;16(1):14-9. Epub 2006 Nov 22. PMID:17123960
Page seeded by OCA on Sun Jul 27 21:55:24 2008
