...
首页> 外文期刊>Biochemistry >Interactions of hexafluoro-2-propanol with the Trp-cage peptide
【24h】

Interactions of hexafluoro-2-propanol with the Trp-cage peptide

机译:六氟-2-丙醇与TRP笼肽的相互作用

获取原文
获取原文并翻译 | 示例
           

摘要

Fluoro alcohols present in aqueous solutions can alter the dominant conformations of peptides and proteins. The origins of these effects likely are related to the details of solute-fluoro alcohol interactions. Preferential interaction of the fluoro alcohol component of a fluoro alcohol-water mixture with peptide solutes has been demonstrated by several experimental approaches. In the present work, we have used H-1{F-19} intermolecular NOE experiments to examine interactions of hexafluoro-2-propanol in a 30% fluoro alcohol-50 mM phosphate buffer solvent mixture with the "Trp-cage" peptide (NLY IQW LKD GGP SSG RPP PS). The results show that the peptide is selectively solvated by hexafluoro-2-propanol to the extent that the fluoro alcohol concentration near the peptide may be 3 to 4 times higher than the nominal concentration of fluoro alcohol in the bulk sample. The observed NOEs indicate that peptide-fluoro alcohol interactions persist for times of the order of 1 ns at 5 degrees C. As the sample temperature is increased, the lifetimes of fluoro alcohol interactions with several exposed side chains decrease to the extent that the peptide hydrogen-solvent fluorine interactions appear to become diffusive in nature, with interaction lifetimes of similar to 0.03 ns. It is known that protein molecules can provide specific sites for binding small organic solvent molecules. Our work suggests that small peptides also have this ability and that the dynamics for such interactions can be site-specific.
机译:存在于水溶液中的氟醇可以改变肽和蛋白质的显性构象。这些效果的起源可能与溶质 - 氟醇相互作用的细节有关。通过几种实验方法证明了氟醇 - 水混合物与肽溶质的氟醇组分的优先相互作用。在本作本作中,我们使用了H-1 {F-19}分子间NOE实验,以与“TRP-CAGE”肽(TRP-CAGE)肽( Nly IQW LKD GGP SSG RPP PS)。结果表明,肽通过六氟-2-丙醇选择性溶剂化,以至于肽附近的氟醇浓度可以比散装样品中的氟醇的标称浓度高出3至4倍。观察到的NOES表明肽 - 氟醇相互作用在5摄氏度下持续1ns的顺序。随着样品温度的增加,氟醇相互作用与几个暴露的侧链的寿命降低至肽氢的程度 - 溶剂氟相互作用似乎在自然中扩散,相互作用的寿命与0.03 ns相似。已知蛋白质分子可以提供用于结合小有机溶剂分子的特异性位点。我们的作品表明,小肽也具有这种能力,并且这种相互作用的动态可以是特定于目的。

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