2jm0
From Proteopedia
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'''Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core'''<br /> | '''Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 2JM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vhp]] | [[Category: vhp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:53:09 2008'' |
Revision as of 12:53, 23 January 2008
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Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core
Overview
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.
About this Structure
2JM0 is a Single protein structure of sequence from [1]. Full crystallographic 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
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