当前位置: X-MOL 学术Mol. Biol. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Investigation of the conformational lability of serum albumin macromolecules in aqueous solution by the NMR spin-echo method.
Molecular Biology ( IF 1.2 ) Pub Date : 1975-01-01
S I Aksenov , O A Kharchuk

The complex proton spin-echo decay curve was recorded for human serum albumin (SA) solutions with different concentrations in normal and heavy water. The curve included three fast-decaying components for SA, in addition to the slow-decaying component for the water. The total amplitude of these three components roughly corresponded to the number of protons in the SA (with isotopic exchange taken into account); the component ratio remained constant at different concentrations and different temperatures between 4 and 39 degrees. The relatively slow-decaying protein component, which accounted for similar to 10% of the SA protons, was produced by the side chains of the protein. The presence of two other faster-decaying SA components with approximately equal amplitudes indicated that only about half of the remaining protons in the SA macromolecule are incorporated into the comparatively rigid globule, the other half belonging to groups with high conformational lability in aqueous solution. The activation energy for the aqueous component was close to that for pure water, while the activation energies for the protein components were roughly twice as large.

中文翻译:

NMR自旋回波法研究水溶液中血清白蛋白大分子的构象不稳定性。

记录了在正常和重水中不同浓度的人血清白蛋白(SA)溶液的复杂质子自旋回波衰减曲线。该曲线除了水的缓慢衰减成分外,还包括SA的三个快速衰减成分。这三个分量的总振幅大致对应于SA中的质子数(考虑了同位素交换);在4到39度之间的不同浓度和不同温度下,组分比保持恒定。衰变相对较慢的蛋白质成分(约占SA质子的10%)是由蛋白质的侧链产生的。存在两个具有近似相等振幅的快速衰变的SA组分表示SA大分子中仅约一半的剩余质子被掺入到相对刚性的球状体中,另一半属于在水溶液中具有高构象不稳定性的基团。水性组分的活化能接近纯水,而蛋白质组分的活化能大约是纯水的两倍。
更新日期:2019-11-01
down
wechat
bug