...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Stability of the C-terminal peptide of CETP mediated through an (i, i + 4) array
【24h】

Stability of the C-terminal peptide of CETP mediated through an (i, i + 4) array

机译：通过（i，i + 4）阵列介导的CETP C末端肽的稳定性

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

Based on circular dichroism (CD), we have found an essential (i, i + 4) α-helix stabilizing array in the C-terminus region for the cholesteryl ester transfer protein (CETP) between histidine 466 and aspartic acid 470. This region apparently corresponds to an amphipathic α-helix. The behavior of this peptide in solution in comparison with a mutant peptide (D_(470)N) was also analyzed by dynamic light scattering (DLS). The results showed that α-helix stabilization is not due to peptide aggregation. The thermodynamic estimation of stability supports the idea that the phenomenon is carried out through an (i, i + 4) array. The representation of the C-terminal region as an amphipathic α-helical peptide shows that lipid-binding activity might be in part due to both the asymmetric polaron-polar residue distribution and to the presence of an (i, i + 4) array important for helix stability.
机译：基于圆二色性（CD），我们在组氨酸466和天冬氨酸470之间的胆固醇酯转移蛋白（CETP）的C端区域发现了必不可少的（i，i + 4）α-螺旋稳定阵列。显然对应于两亲性α-螺旋。还通过动态光散射（DLS）分析了该肽与突变体肽（D_（470）N）相比在溶液中的行为。结果表明，α-螺旋稳定化不是由于肽聚集。稳定性的热力学估计支持以下观点：通过（i，i + 4）阵列执行该现象。 C末端区域表示为两亲性α-螺旋肽，表明脂质结合活性可能部分是由于非对称极性/非极性残基分布以及（i，i + 4）的存在阵列对于螺旋稳定性很重要。

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