N,O-dideuterio-N-(N,N-dideuterio-glycyl)-glycine | 24720-25-0

• 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: N,O-dideuterio-N-(N,N-dideuterio-glycyl)-glycine
• 英文别名: N,O-dideuterio-N-(N,N-dideuterio-glycyl)-glycine
• CAS: 24720-25-0
• 化学式: C₄H₈N₂O₃
• 分子量: 136.087
• InChiKey: YMAWOPBAYDPSLA-JBISRTOLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.91
• 重原子数：
  9.0
• 可旋转键数：
  4.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  96.87
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  N,O-dideuterio-N-(N,N-dideuterio-glycyl)-glycine 在 硝酸 作用下， 以 重水 为溶剂， 生成
  参考文献：
  名称：

  A study of hydrogen-bonding of amino acids, peptides and polypeptides in the solid state as a function of temperature by static 2H NMR method

  摘要：

  H-2 NMR spectra of H-2-labeled amino acids, peptides, and polypeptides, as prepared in this work, were measured in the solid state over a wide range of temperatures. From spectral simulations based on the 2H dynamic NMR theory, NMR parameters such as quadrupolar coupling constant (e(2)qQ/h) and electric field gradient asymmetric parameter (eta) were determined, and the relationship between these NMR parameters and the hydrogen-bond length (R-N...(O)) was elucidated. From the observed H-2 NMR spectra of amide (NH)-H-2 deuteron of peptides and polypeptides in the solid state, it was found that the e(2)qQ/h values decrease with a decrease in R-N...(O). This shows that the hydrogen-bond length of peptides and polypeptides can be evaluated through the observation of the e(2)qQ/h value of the amide deuteron. Further, the observed H-2 NMR spectra of the (NH3)-H-2 deuterons of H-2-labeled Gly and GlyGly in the solid state, as a function of temperature, were analyzed with spectral simulations. From this result, the rotational barrier around the C-alpha-(NH3)-H-2 bond was determined. On the other hand, from the observation of H-2 NMR spectra of H-2-labeled GlyGly.HNO3 and GlyGly.H2O.HCl in the solid state, it was found that the rate of the C-3nu rotation around the C-alpha-NH3 of these compounds is several MHz above in the temperature range 215-340 K, and is higher than that observed for H-2-labeled GlyGly. (C) 2002 Elsevier Science B.V. All rights reserved.

  DOI：

  10.1016/s0022-2860(01)00770-0
• 作为产物：
  描述：

  双甘肽 以 重水 为溶剂， 反应 168000.0h， 生成 N,O-dideuterio-N-(N,N-dideuterio-glycyl)-glycine
  参考文献：
  名称：

  A study of hydrogen-bonding of amino acids, peptides and polypeptides in the solid state as a function of temperature by static 2H NMR method

  摘要：

  H-2 NMR spectra of H-2-labeled amino acids, peptides, and polypeptides, as prepared in this work, were measured in the solid state over a wide range of temperatures. From spectral simulations based on the 2H dynamic NMR theory, NMR parameters such as quadrupolar coupling constant (e(2)qQ/h) and electric field gradient asymmetric parameter (eta) were determined, and the relationship between these NMR parameters and the hydrogen-bond length (R-N...(O)) was elucidated. From the observed H-2 NMR spectra of amide (NH)-H-2 deuteron of peptides and polypeptides in the solid state, it was found that the e(2)qQ/h values decrease with a decrease in R-N...(O). This shows that the hydrogen-bond length of peptides and polypeptides can be evaluated through the observation of the e(2)qQ/h value of the amide deuteron. Further, the observed H-2 NMR spectra of the (NH3)-H-2 deuterons of H-2-labeled Gly and GlyGly in the solid state, as a function of temperature, were analyzed with spectral simulations. From this result, the rotational barrier around the C-alpha-(NH3)-H-2 bond was determined. On the other hand, from the observation of H-2 NMR spectra of H-2-labeled GlyGly.HNO3 and GlyGly.H2O.HCl in the solid state, it was found that the rate of the C-3nu rotation around the C-alpha-NH3 of these compounds is several MHz above in the temperature range 215-340 K, and is higher than that observed for H-2-labeled GlyGly. (C) 2002 Elsevier Science B.V. All rights reserved.

  DOI：

  10.1016/s0022-2860(01)00770-0

文献信息

• Formation and Stability of Peptide Enolates in Aqueous Solution
  作者：Ana Rios、John P. Richard、Tina L. Amyes

  DOI：10.1021/ja026267a

  日期：2002.7.1

  log k(HO) and carbon acid pK(a) established in earlier work for deprotonation of related neutral and cationic alpha-carbonyl carbon acids. The alpha-amino carbon at a N-protonated N-terminus of a peptide or protein is estimated to undergo deprotonation about 130-fold faster than the alpha-amino carbon at the corresponding internal amino acid residue. The value of k(HO) for deprotonation of the N-terminal

  二阶速率常数 k(DO) (M(-1) s(-1)) 在 D(2)O 中确定，用于甘氨酰甘氨酸和甘氨酰甘氨酰甘氨酸两性离子的 N 端 α-氨基碳的去质子化，内部α-甘氨酰甘氨酰甘氨酸阴离子的氨基碳，以及 N-乙酰甘氨酸阴离子和 N-乙酰甘氨酰胺的乙酰甲基和α-氨基碳被氘化离子。该数据用于估计 k(H2O) (M(-1) s(-1)) 的值，用于从这些碳酸到 H(2)O 中的氢氧根离子的质子转移。这些碳酸的 pK(a) 值范围为 23.9 至 30.8，是通过对 log k( ) 和碳酸 pK(a) 之间良好线性相关性的内插或外推获得的，这些相关性在早期相关中性和阳离子去质子化工作中建立α-羰基碳酸。据估计，肽或蛋白质的 N 质子化 N 末端的 α-氨基碳比相应内部氨基酸残基处的 α-氨基碳快约 130 倍进行去质子化。甘氨酰甘氨酰甘氨酸两性离子 N 端 α-氨基碳去质子化的 k( )
• Morowitz; Chapman, Archives of Biochemistry, 1955, vol. 56, p. 110,111,112
  作者：Morowitz、Chapman

  DOI：——

  日期：——
• Rosenberg, Acta Chemica Scandinavica (1947), 1957, vol. 11, p. 1390,1391
  作者：Rosenberg

  DOI：——

  日期：——