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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure, thermostability, and conformational flexibility of hen egg-white lysozme dissolved in glycerol
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Structure, thermostability, and conformational flexibility of hen egg-white lysozme dissolved in glycerol

机译：溶解在甘油中的蛋清溶菌酶的结构，热稳定性和构象柔韧性

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摘要

Hen egg-white lysozyme dissolved in glycerol containing 1 water was studied by using CD and amide proton exchange monitored by two-dimensional 1H NMR. The far- and near-FV CD spectra of the protein showed that the secondary and tertiary structures of lysozyme in glycerol were similar to those in water. Thermal melting of lysozyme in glyccrol followed by CD spectral changes indicated unfolding of the tertiary structure with a TM of 76.0 ± 0.2 deg.C and no appreciable loss of the secondary structure up to 85 deg. C. This is in contrast to the coincident denaturation of both tertiary and secondary structures with T_m values of 74.8 + - 0.4 deg C and 74.3 + - 0.7 deg. C, respectively, under analogous conditions in water. Quenched amide Proton exchange experiments re- vealed a greater structural protection of amide protons in glycerol than in water for a majority of the slowly exchanging protons. The results point to a highly ordered, native-like structure of lysozyme in glycerol, with the stability exceeding that in water.
机译：通过使用CD和通过二维1H NMR监测的酰胺质子交换，研究了溶解在含有1水的甘油中的鸡蛋清溶菌酶。该蛋白质的远近FV CD谱表明，甘油中溶菌酶的二级和三级结构与水中的相似。甘醇中溶菌酶的热融化，随后CD光谱变化表明三级结构的展开，TM为76.0±0.2℃，直到85℃二级结构没有明显损失。这与T_m值为74.8±0.4℃和74.3±0.7℃的三级和二级结构的同时变性相反。 C分别在类似条件下在水中。淬灭的酰胺质子交换实验表明，对于大多数缓慢交换的质子，甘油中的酰胺质子比在水中的结构质保护性更高。结果表明，溶菌酶在甘油中具有高度有序的天然样结构，其稳定性超过了在水中的稳定性。

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