Jarema M A, Lu P, Miller J H
Proc Natl Acad Sci U S A. 1981 May;78(5):2707-11. doi: 10.1073/pnas.78.5.2707.
By using a systematic genetic approach, the resonances in the 19F NMR spectrum of 3-fluorotyrosine-substituted lac repressor protein have been assigned. The NMR data indicate that each monomer of the repressor consists of two distinct and independent domains. One domain, the NH2-terminal sixth of the primary sequence, which has been shown to be very important for DNA binding, is very mobile. The remaining COOH-terminal sequence is more rigid. Ligands of the repressor, which affect its DNA binding capability, lead to conformational changes in the COOH-terminal domain. The approach to the assignment of spectral features taken here can be extended to other systems.
通过使用系统遗传学方法,已确定了3-氟酪氨酸取代的乳糖阻遏蛋白的19F NMR谱中的共振峰。NMR数据表明,阻遏蛋白的每个单体由两个不同且独立的结构域组成。一个结构域是一级序列的NH2末端六分之一,已证明其对DNA结合非常重要,且非常灵活。其余的COOH末端序列则更为刚性。影响其DNA结合能力的阻遏蛋白配体会导致COOH末端结构域发生构象变化。此处采用的光谱特征归属方法可扩展到其他系统。