Tang Yi, Ghirlanda Giovanna, Petka Wendy A, Nakajima Tadashi, DeGrado William F, Tirrell David A
Division of Chemistry and Chemical Engineering California Institute of Technology Pasadena, CA 91125 (USA) Fax: (+1) 626-793-8472.
Department of Biochemistry & Biophysics University of Pennsylvania Philadelphia, PA 19104 (USA).
Angew Chem Int Ed Engl. 2001 Apr 17;40(8):1494-1496. doi: 10.1002/1521-3773(20010417)40:8<1494::AID-ANIE1494>3.0.CO;2-X.
Fluorination of the hydrophobic core of a coiled-coil protein significantly improved its stability toward thermal and chemical denaturation. 5',5',5'-Trifluoroleucine (2) was efficiently incorporated into a leucine-zipper protein in place of leucine (1) during E. coli biosynthesis. The fluorinated variant maintained stable secondary and tertiary structures under conditions that caused denaturation of the "wild-type" protein.
对卷曲螺旋蛋白的疏水核心进行氟化，可显著提高其对热变性和化学变性的稳定性。在大肠杆菌生物合成过程中，5',5',5'-三氟亮氨酸（2）有效地取代亮氨酸（1）掺入到亮氨酸拉链蛋白中。在导致“野生型”蛋白变性的条件下，氟化变体保持了稳定的二级和三级结构。
