N.m.r. analyses of the histidine microenvironments in a human salivary proline-rich glycoprotein.

N.m.r. analyses of the histidine microenvironments in a human salivary proline-rich glycoprotein.
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N.m.r.

DOI:
10.1111/j.1399-3011.1988.tb00672.x
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发表时间:
1988
期刊:
International journal of peptide and protein research
影响因子:
--
通讯作者:
Levine,MJ
Levine,MJ
中科院分区:
--
文献类型:
--
作者:
Loomis,RE;Tseng,CC;Levine,MJ

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通过 360 MHz 质子核磁共振测定人腮腺唾液 (PRG) 富含脯氨酸的糖蛋白中三个组氨酸残基的 pKa。光谱学。添加钙 (0.64 mm) 导致所有三种组氨酸的 pKa 下降约 0.25 个单位。当咪唑和环(L-组氨酸-L-脯氨酸)用作模型化合物时,相应浓度的钙对其 pKa 没有影响。此外,模型化合物给出的绝对 pKa 值与文献中报道的类似化学物质非常一致。交换寿命数据和先前报道的氢→氘交换实验表明PRG组氨酸NtH质子不参与氢键。总的来说,这些数据表明添加钙后 PRG 构象发生变化。
The pKa's of the three histidine residues in a proline‐rich glycoprotein from human parotid saliva (PRG) were determined by 360 MHz proton n.m.r. spectroscopy. The addition of calcium (0.64 mm) caused drops in the pKa's of all three histidines by ∼0.25 units. When imidazole and cyclo(l‐histidine‐l‐proline) were used as model compounds, corresponding concentrations of calcium had no effect on their pKa's. Also, the model compounds gave absolute pKavalues in good agreement with similar chemical species reported in the literature. Exchange lifetime data and previously reported hydrogen → deuterium exchange experiments suggest that the PRG histidine NtH protons are not involved in hydrogen‐bonds. Collectively, these data imply that changes in PRG conformation occur upon the addition of calcium.
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