Stabilizing and Destabilizing Effects of Phenylalanine F5-Phenylalanine Mutations on the Folding of a Small Protein
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- 作者：Matthew G. Woll ; Erik B. Hadley ; Sandro Mecozzi ; Samuel H. Gellman
- 刊名：Journal of the American Chemical Society
- 出版年：2006
- 出版时间：December 20, 2006
- 年：2006
- 卷：128
- 期：50
- 页码：15932 - 15933
- 全文大小：94K
- 年卷期：v.128,no.50(December 20, 2006)
- ISSN：1520-5126
文摘
We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe G SRC="/images/entities/rarr.gif"> 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 
ges/entities/rarr.gif"> 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 ges/entities/rarr.gif"> F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability.