934740-49-5Relevant academic research and scientific papers
Stabilizing and destabilizing effects of phenylalanine → F 5-phenylalanine mutations on the folding of a small protein
Woll, Matthew G.,Hadley, Erik B.,Mecozzi, Sandro,Gellman, Samuel H.
, p. 15932 - 15933 (2007/10/03)
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. Copyright
