...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >INTERNAL MOBILITY IN THE PARTIALLY FOLDED DNA BINDING AND DIMERIZATION DOMAINS OF GAL4 - NMR ANALYSIS OF THE N-H SPECTRAL DENSITY FUNCTIONS
【24h】

INTERNAL MOBILITY IN THE PARTIALLY FOLDED DNA BINDING AND DIMERIZATION DOMAINS OF GAL4 - NMR ANALYSIS OF THE N-H SPECTRAL DENSITY FUNCTIONS

机译：GAL4部分折叠的DNA结合和二聚化域的内部流动性-N-H光谱密度函数的分析

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The DNA binding domain (residues 1-65) of the yeast transcriptional activator GAL4 is only partially folded. While residues 10-41, the DNA recognition domain, form a well-defined structure in the free protein, the whole polypeptide folds up and dimerizes upon binding DNA. In order to describe the mobility of the protein, we have characterized the frequency spectrum of the motions of N-H bond vectors of GAL4(1-65) using a reduced spectral density mapping approach (an approximation of the full spectral density mapping technique) [Peng, J. W., & Wagner, G, (1992a) J. Magn. Reson. 98, 308-332; Peng, J. W., & Wagner, G, (1992b) Biochemistry 31, 8571-8586]. N-15 spin-lattice relaxation [R(N)(N-z)], spin-spin relaxation [R(N)(N-x,N-y)], cross-relaxation [R(N)(H-z --> N-z)], two-spin order [R(NH)(2H(z)N(z))], and antiphase [R(NH)(2H(z)N(x,y))] rates were determined for 52 of the 65 backbone amide groups at 10 degrees C anti pH 6.5 at 11.74 T. Calculations of the spectral density functions using a reduced set of R(N)(N-z), R(N)(N-x,N-y), R(N)(H-z --> N-z), and R(NH)(2H(z)N(z)) gave excellent agreement with those calculated using all six sets. The reduced method has the added advantage that the errant behavior seen at high field values is circumvented, A linear correlation was found between J(omega(N)) and J(0) with a limited and clearly defined range of J(0) values which defines the range of rates for internal motions in GAL4(1-65). It appears that all residues experience a combination of two movements: one of the overall tumbling (correlation time, 8.65 ns) and the other of fast internal fluctuations of the structure. The respective weights of these contributions vary with the primary sequence and faithfully mirror the secondary and tertiary elements of the protein. The position on the correlation line of J(omega(N)) versus J(0) indicates the amount of angular averaging relative to the overall motion of the protein. A spectral density function for internal motions can be described.
机译：酵母转录激活物GAL4的DNA结合结构域（残基1-65）仅被部分折叠。尽管残基10-41（DNA识别域）在游离蛋白中形成了明确定义的结构，但整个多肽会折叠并在结合DNA时二聚。为了描述蛋白质的迁移率，我们使用简化的谱密度映射方法（近似于全谱密度映射技术）表征了GAL4（1-65）NH键载体运动的频谱。 ，JW，＆Wagner，G，（1992a）J.Magn.Chem.Soc。，66，1955，1959。雷森98，308-332; Peng，J.W。，＆Wagner，G，（1992b）Biochemistry 31，8571-8586]。 N-15个自旋晶格弛豫[R（N）（Nz）]，自旋自旋弛豫[R（N）（Nx，Ny）]，交叉松弛[R（N）（Hz-> Nz）]，确定了65个主干中的52个主旋律的二旋顺序[R（NH）（2H（z）N（x，y））]和反相[R（NH）（2H（z）N（x，y））]速率酰胺基团在10摄氏度，抗pH 6.5和11.74 T下使用减少的R（N）（Nz），R（N）（Nx，Ny），R（N）（Hz- > Nz），并且R（NH）（2H（z）N（z））与使用全部六组计算的结果非常吻合。简化方法的另一个优点是可以避免在高场值下出现的错误行为，并且在J（omega（N））和J（0）之间发现了线性相关性，并且J（0）值的范围很有限它定义了GAL4（1-65）中内部运动的速率范围。看来所有残渣都经历两种运动的组合：一种是整体翻滚（相关时间为8.65 ns），另一种是结构的内部快速波动。这些贡献的权重随一级序列而变化，忠实地反映了蛋白质的二级和三级元素。 J（ω（N））对J（0）的相关线上的位置表示相对于蛋白质整体运动的角度平均量。可以描述内部运动的频谱密度函数。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号