...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Protein stability function relations: beta-lactoglobulin-A sulphydryl group reactivity and its relationship to protein unfolding stability
【24h】

Protein stability function relations: beta-lactoglobulin-A sulphydryl group reactivity and its relationship to protein unfolding stability

机译：蛋白质稳定性功能关系：β-乳球蛋白-A硫代基团反应性及其与蛋白质展开稳定性的关系

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 effect of protein stability on the reactivity of the free sulphydryl (SH) group in beta-lactoglobulin-A (beta-LgA) provides a model for the study of protein stability-function relations (PSFR). The free energy change for protein unfolding (Delta G(O)) and SH group exposure (Delta G(SH)) were determined from (i) the urea unfolding curve for beta-LgA and (ii) the kinetics of beta-LgA SH/disulphide exchange with 2-pyridine disulphide (2-PDS) in 0-8 M urea (pH 3). Protein unfolding profiles determined from extrinsic fluorescence and SH-group reactivity measurements were not coincident. beta-LgA formed a stable intermediate (X) state in the presence of 4 M urea with Delta G(O) = 20 (+/- 0.03) kJ/mol. From the low rate of SH/disulphide exchange in 4 M urea, the SH-group within beta-LgA was efficiently masked within the X-state. SH reactivity increased after beta-LgA was unfolded in 6-8 M urea with, Delta G(SH) = 43( +/- 6.4) kJ/mol. Such results are discussed in terms of possible interrelationships between protein unfolding stability and SH reactivity in beta-LgA. (C) 1998 Elsevier Science B.V. All rights reserved. [References: 46]
机译：蛋白质稳定性对β-乳球蛋白-A（β-LgA）中游离巯基（SH）基反应性的影响为蛋白质稳定性-功能关系（PSFR）的研究提供了模型。从（i）β-LgA的尿素展开曲线和（ii）β-LgASH的动力学确定蛋白质解折叠的自由能变化（Delta G（O））和SH组暴露（Delta G（SH））在0-8 M尿素（pH 3）中与2-吡啶二硫化物（2-PDS）进行二硫化物交换。从外部荧光和SH组反应性测量确定的蛋白质展开图不是一致的。在存在4 M尿素且Delta G（O）= 20（+/- 0.03）kJ / mol的条件下，β-LgA形成稳定的中间体（X）状态。由于在4 M尿素中SH /二硫化物交换率低，β-LgA中的SH-基团被有效地掩盖在X-状态中。 β-LgA在6-8 M尿素中展开后，SH反应性增加，Delta G（SH）= 43（+/- 6.4）kJ / mol。就β-LgA中蛋白质展开稳定性和SH反应性之间可能的相互关系讨论了这种结果。 （C）1998 Elsevier Science B.V.保留所有权利。 [参考：46]

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