Ac-CREVTVNGKTIWQC | 1214191-69-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Ac-CREVTVNGKTIWQC
• CAS: 1214191-69-1
• 化学式: C₇₁H₁₁₃N₂₁O₂₂S₂
• 分子量: 1676.94
• InChiKey: AQMDSVYUEOFFKR-LDTNGYFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.85
• 重原子数：
  116.0
• 可旋转键数：
  26.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  712.35
• 氢给体数：
  25.0
• 氢受体数：
  24.0

反应信息

• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-缬氨酸 、 乙酸酐 、 Fmoc-L-异亮氨酸 、 Fmoc-L-色氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 哌啶 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.17h， 生成 Ac-CREVTVNGKTIWQC
  参考文献：
  名称：

  Controlling Peptide Folding with Repulsive Interactions between Phosphorylated Amino Acids and Tryptophan

  摘要：

  Phosphorylated amino acids were incorporated into a designed beta-hairpin peptide to study the effect on beta-hairpin structure when the phosphate group is positioned to interact with a tryptophan residue on the neighboring strand. The three commonly phosphorylated residues in biological systems, serine, threonine, and tyrosine, were studied in the same beta-hairpin system. It was found that phosporylation destabilizes the hairpin structure by approximately 1.0 kcal/mol, regardless of the type of phosphorylated residue. In contrast, destabilization due to glutamic acid was about 0.3 kcal/mol. Double mutant cycles and pH studies are consistent with a repulsive interaction as the source of destabilization. These findings demonstrate a novel mechanism by which phosphorylation may influence protein structure and function.

  DOI：

  10.1021/ja9047575