Stabilizing and destabilizing effects of phenylalanine --> F5-phenylalanine mutations on the folding of a small protein |
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Authors: | Woll Matthew G Hadley Erik B Mecozzi Sandro Gellman Samuel H |
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Institution: | Department of Chemistry and School of Pharmacy, University of Wisconsin, Madison, Wisconsin 53706, USA. |
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Abstract: | We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe --> F5-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 --> F5-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl-aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 --> F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability. |
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