| 959709-65-0

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• CAS: 959709-65-0
• 化学式: C₆₅H₁₁₃N₁₉O₁₆
• 分子量: 1417.72
• InChiKey: TWAGPOZLRIFCKR-UCQFVPJESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.82
• 重原子数：
  100.0
• 可旋转键数：
  49.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  603.77
• 氢给体数：
  21.0
• 氢受体数：
  19.0

反应信息

• 作为产物：
  描述：

  N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine 、 Fmoc-甘氨酸 、 Fmoc-L-酪氨酸 、 Fmoc-2-氨基异丁酸 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 生成
  参考文献：
  名称：

  Cross-Strand Coupling of a β-Hairpin Peptide Stabilized with an Aib-Gly Turn Studied Using Isotope-Edited IR Spectroscopy

  摘要：

  Isotope-edited IR spectroscopy was used to study a series of singly and doubly C-13=O-labeled beta-hairpin peptides stabilized by an Aib-Gly turn sequence. The double-labeled peptides have amide I' IR spectra that show different degrees of vibrational coupling between the C-13-labeled amides due to variations in the local geometry of the peptide structure. The single-labeled peptides provide controls to determine frequencies characteristic of the diagonal force field (FF) contributions at each position for the uncoupled C-13=O modes. Separation of diagonal FF and coupling effects on the spectra are used to explain the cross-strand labeled spectral patterns. DFT calculations based on an idealized model beta-hairpin peptide correctly predict the vibrational coupling patterns. Extending these model results by consideration of frayed ends and the hairpin conformational flexibility yields an alternate interpretation of details of the spectra. Temperature-dependent isotopically labeled IR spectra reveal differences in the thermal stabilities of the individual isotopically labeled sites. This is the first example of using an IR-based isotopic labeling technique to differentiate structural transitions at specific sites along the peptide backbone in model beta-hairpin peptides.

  DOI：

  10.1021/ja0736414