Ac-RpYVTVNG-NH2 | 1214175-11-7

• 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-RpYVTVNG-NH2
• CAS: 1214175-11-7
• 化学式: C₃₇H₆₁N₁₂O₁₄P
• 分子量: 928.937
• InChiKey: DCNUMVJDMDXETC-KFJPORACSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.94
• 重原子数：
  64.0
• 可旋转键数：
  27.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  438.77
• 氢给体数：
  15.0
• 氢受体数：
  13.0

反应信息

• 作为产物：
  描述：

  Fmoc-L-缬氨酸 、 乙酸酐 、 (S)-2-((((9H-芴-9-基)甲氧基)羰基)氨基)-3-(4-((双(苄氧基)磷酰基)氧基)苯基)丙酸 、 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 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-RpYVTVNG-NH2
  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