Small-angle neutron scattering study of protein unfolding and refolding
Small-angle neutron scattering study of protein unfolding and refolding
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DOI：
10.1103/physreve.80.011924
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发表时间：
2009-07-01
影响因子：
2.4
通讯作者：
Wagh, A. G.
中科院分区：
文献类型：
--
作者：
Aswal, V. K.;Chodankar, S.;Wagh, A. G.
小角中子散射已被用来研究蛋白质去折叠和重折叠的蛋白质牛血清白蛋白（BSA）由于其天然结构的扰动引起的三种不同的蛋白质变性剂：尿素，表面活性剂，和压力。BSA蛋白在尿素浓度大于4 M时展开，并且观察到与蛋白浓度无关。表面活性剂的添加通过沿着蛋白质的展开多肽链形成表面活性剂的胶束状聚集体来展开蛋白质，并且取决于表面活性剂与蛋白质浓度的比率。我们利用稀释法显示了在尿素和表面活性剂存在下未折叠蛋白质的重折叠。BSA在高达450 MPa的压力下不显示任何蛋白质解折叠。尿素和表面活性剂的存在下（浓度之前，诱导自己的解折叠）已被用来检查在较低的压力下的蛋白质的压力诱导的解折叠。在存在尿素的情况下，蛋白质在200 MPa的压力下解折叠;然而，使用表面活性剂时没有观察到解折叠。在所有上述变性方法中，蛋白质去折叠被证明是可逆的。
Small-angle neutron scattering has been used to study protein unfolding and refolding in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by three different protein denaturating agents: urea, surfactant, and pressure. The BSA protein unfolds for urea concentrations greater than 4 M and is observed to be independent of the protein concentration. The addition of surfactant unfolds the protein by the formation of micellelike aggregates of surfactants along the unfolded polypeptide chains of the protein and depends on the ratio of surfactant to protein concentration. We make use of the dilution method to show the refolding of unfolded proteins in the presence of urea and surfactant. BSA does not show any protein unfolding up to the pressure of 450 MPa. The presence of urea and surfactant (for concentrations prior to inducing their own unfolding) has been used to examine pressure-induced unfolding of the protein at lower pressures. The protein unfolds at 200 MPa pressure in the presence of urea; however, no unfolding is observed with surfactant. The protein unfolding is shown to be reversible in all the above denaturating methods.