• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >MAIN-CHAIN DYNAMICS OF A PARTIALLY FOLDED PROTEIN - N-15 NMR RELAXATION MEASUREMENTS OF HEN EGG WHITE LYSOZYME DENATURED IN TRIFLUOROETHANOL
【24h】

MAIN-CHAIN DYNAMICS OF A PARTIALLY FOLDED PROTEIN - N-15 NMR RELAXATION MEASUREMENTS OF HEN EGG WHITE LYSOZYME DENATURED IN TRIFLUOROETHANOL

机译：部分折叠蛋白质在三氟乙醇中变性的鸡卵白溶菌酶的主链动力学-N-15 NMR弛豫测量

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

N-15 NMR relaxation measurements have been used to study the dynamic behaviour of the main-chain of hen lysozyme in a partially folded state, formed in a 70% (v/v) trifluoroethanol (TFE)/30% water mixture at 37 degrees C and pH 2. This state is characterised by helical secondary structure in the absence of extensive tertiary interactions. The NMR relaxation data were interpreted by mapping of spectral density functions and by derivation of segmental as well as global order parameters. The results imply that the dynamics of lysozyme in TFE can, at least for the great majority of residues, be adequately described by internal motions which are superimposed on an overall isotropic tumbling of the molecule. Although the dynamic behaviour shows substantial variations along the polypeptide chain, it correlates well with the conformational preferences identified in the TFE state by other NMR parameters. Segments of the polypeptide chain which are part of persistent helical structures are highly restricted in their motion (S-2 > 0.8, with effective internal correlation times tau(e) < 200 ps) but are also found to experience conformational exchange on a millisecond timescale. Regions which are stabilised in less persistent helical structure possess greater flexibility (0.6 < S-2 < 0.8, 200 ps < tau(e) < 1 ns) and those which lack defined conformational preferences are highly flexible (S-2 < 0.6, tau(e) similar to 1 ns). The dynamic behaviour of the main-chain was found to be correlated with other local features of the polypeptide chain, including hydrophobicity and the position of the disulphide bridges. Despite the absence of extensive tertiary interactions, preferential stabilisation of native-like secondary structure by TFE results in a pattern of main-chain dynamics which is similar to that of the native state. (C) 1996 Academic Press Limited [References: 58]
机译：N-15 NMR弛豫测量已用于研究在70％（v / v）三氟乙醇（TFE）/ 30％水混合物中于37度形成的部分折叠状态的鸡溶菌酶主链的动力学行为C和pH2。该状态的特征是在没有广泛的三级相互作用的情况下呈螺旋二级结构。 NMR弛豫数据通过谱密度函数的映射以及分段以及全局顺序参数的推导来解释。结果表明，至少对于大多数残基，TFE中溶菌酶的动力学可以通过叠加在分子总体各向同性翻转上的内部运动来充分描述。尽管动力学行为沿多肽链显示出很大的变化，但它与通过其他NMR参数在TFE状态中识别的构象偏好密切相关。作为永久螺旋结构一部分的多肽链片段的运动受到严格限制（S-2> 0.8，有效内部相关时间tau（e）<200 ps），但也发现在毫秒级的时间进行构象交换。在不太持久的螺旋结构中稳定的区域具有更大的柔韧性（0.6

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