• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文学位 >Study of a Model alpha-Helix Peptide's Surface Properties by Langmuir Monolayer Techniques and Surface FTIR
【24h】

Study of a Model alpha-Helix Peptide's Surface Properties by Langmuir Monolayer Techniques and Surface FTIR

机译：用Langmuir单层技术和表面FTIR研究α-螺旋模型肽的表面性质。

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

Cell membranes have been shown to be able to change the conformation of proteins/peptides. However, the structure of the cell membrane is complicated and has been divided to three regions: the hydrophobic region containing alkyl chains, the hydrophilic head group, and the hydration layer, or lipid-water interface, which exists between the hydrophilic head group and the bulk water solution, but with lower dielectric constant compared with fully hydrated water. The air-water interface has been used to mimic the structure of the hydration layer because of their similar dielectric constant.1,2 Some proteins were found to form a stable Langmuir monolayer and accumulate at the air-water interface. For example, ?-synclein, a membrane protein containing 140 amino acids, is unstructured in aqueous solution but changes its conformation to alpha-helix at the air-water interface. This incites interest to investigate short motifs of alpha-helix to form a stable Langmuir monolayer at the air-water interface. In this thesis, a peptide with sequence of YAAAA(KAAAA)4 (referred as Pep25 hereafter) was used as a model peptide of alpha-helix to spread at the air-water interface, because our group has determined the conformation of Pep25 in residue level by the 13C isotope-edited FTIR. Langmuir monolayer technique together with IRRAS showed that Pep25 does not form a typical Langmuir monolayer at the interface. Potential plans to make Pep25 to form a stable monolayer are also discussed in this thesis.
机译：已经证明细胞膜能够改变蛋白质/肽的构象。然而，细胞膜的结构很复杂，已分为三个区域：包含烷基链的疏水区域，亲水性头基和存在于亲水性头基与亲水性基团之间的水合层或脂质-水界面。大体积水溶液，但与完全水合的水相比介电常数低。空气-水界面因其相似的介电常数而被用于模拟水合层的结构。1,2一些蛋白质被发现形成稳定的Langmuir单层并在空气-水界面处积聚。例如，β-synclein，一种含有140个氨基酸的膜蛋白，在水溶液中没有结构，但在空气-水界面处的构象变为α-螺旋。这引起了研究α-螺旋的短基元以在空气-水界面形成稳定的Langmuir单层的兴趣。本文采用YAAAA（KAAAA）4序列的肽段（以下简称Pep25）作为α-螺旋模型肽在空气-水界面处扩散，因为我们小组已经确定了残基中Pep25的构象。水平由13C同位素编辑的FTIR确定。 Langmuir单层技术与IRRAS一起显示，Pep25在界面处未形成典型的Langmuir单层。本文还讨论了使Pep25形成稳定单层的潜在计划。

著录项

  • 作者

    Combs, J. Dale.;

  • 作者单位

    Middle Tennessee State University.;

  • 授予单位 Middle Tennessee State University.;
  • 学科 Biochemistry.;Analytical chemistry.
  • 学位 M.S.
  • 年度 2016
  • 页码 59 p.
  • 总页数 59
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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