19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles.
19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles.
复制标题
合成磷脂囊泡和脱氧胆酸盐胶束中噬菌体 M13 外壳蛋白的 19F 核磁共振研究。
DOI：
10.1016/s0006-3495(82)84673-0
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发表时间：
1982
影响因子：
3.4
通讯作者：
B. Sykes
中科院分区：
文献类型：
--
作者：
H. Dettman;J. Weiner;B. Sykes
The nonlytic, filamentous coliphage M13 offers an excellent model system for the study of membrane-protein interactions. We prepare derivatives of the protein containing fluorine-labeled amino acids and use 19F nuclear magnetic resonance (NMR) to study the protein in both deoxycholate micelles and phospholipid vesicles. We have previously described the in vivo preparation of an m-fluorotyrosyl derivative of M13 coat protein and also a method for incorporation of high levels of this protein into small, uniformly sized phospholipid vesicles of defined composition. Herein we describe the in vivo preparation and the characterization of an m-fluorophenylalanine derivative. We simultaneously compare the environment and mobility of the tyrosine and phenylalanine residues (the former in the hydrophobic region of the protein and the latter in the hydrophilic regions) as influenced by bile salt detergent or lipid interactions.
