19F nuclear magnetic resonance studies of selectively fluorinated derivatives of G- and F-actin.
19F nuclear magnetic resonance studies of selectively fluorinated derivatives of G- and F-actin.
复制标题
G-和F-肌动蛋白选择性氟化衍生物的19F核磁共振研究。
作者：
M. Brauer;B. Sykes
G-肌动蛋白是一种球状蛋白（Mr 42 300），已知具有三个半胱氨酸残基，至少部分暴露并具有化学反应性（Cys-10、-284和-374）。当G-肌动蛋白与3-溴-1，1，1-三氟丙酮反应时，在19 F NMR谱中观察到三个可分辨的19 F共振。这种氟化的G-肌动蛋白衍生物保持完全可聚合，并且其31 P NMR谱与未修饰的G-肌动蛋白的31 P NMR谱没有显著不同，表明化学修饰没有使肌动蛋白变性，并且修饰的残基不干扰聚合的程度或腺苷5 '-三磷酸的结合。三个19 F共振之一被指定为氟化Cys-374的基础上，其选择性反应与N-乙基马来酰亚胺。这一共振显着拓宽氟化G-肌动蛋白聚合后，而其他两个共振没有显着扩大或移动。因此，Cys-10和Cys-284不参与G-肌动蛋白的聚合，也不受G-肌动蛋白聚合的明显影响，而Cys-374处的19 F标记的迁移率显著降低。
G-Actin is a globular protein (Mr 42 300) known to have three cysteine residues that are at least partially exposed and chemically reactive (Cys-10, -284, and -374). When G-actin was reacted with 3-bromo-1,1,1-trifluoropropanone, three resolvable 19F resonances were observed in the 19F NMR spectrum. This fluorinated G-actin derivative remained fully polymerizable, and its 31P NMR spectrum was not significantly different from that of unmodified G-actin, indicating that the chemical modification did not denature the actin and the modified residues do not interfere with the extent of polymerization or the binding of adenosine 5'-triphosphate. One of the three 19F resonances was assigned to fluorinated Cys-374 on the basis of its selective reaction with N-ethylmaleimide. This resonance was dramatically broadened after polymerization of fluorinated G-actin, while the other two resonances were not markedly broadened or shifted. Thus, Cys-10 and -284 are not involved in or appreciably affected by the polymerization of G-actin, while the mobility of the 19F label at Cys-374 is markedly reduced.
影响因子：
2.9
作者：
Tait,JF;Frieden,C
通讯作者：
Frieden,C
用于骨骼肌 G-肌动蛋白构象变化的荧光探针。
DOI：
--
发表时间：
1980
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Frieden,C;Lieberman,D;Gilbert,HR
通讯作者：
Gilbert,HR