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首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Structure thermostability and conformational flexibility of hen egg-white lysozyme dissolved in glycerol
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Structure thermostability and conformational flexibility of hen egg-white lysozyme dissolved in glycerol

机译：母鸡的结构热稳定性和构象柔韧性 溶解在甘油中的蛋清溶菌酶

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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-UV 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 glycerol followed by CD spectral changes indicated unfolding of the tertiary structure with a Tm of 76.0 ± 0.2°C and no appreciable loss of the secondary structure up to 85°C. This is in contrast to the coincident denaturation of both tertiary and secondary structures with Tm values of 74.8 ± 0.4°C and 74.3 ± 0.7°C, respectively, under analogous conditions in water. Quenched amide proton exchange experiments revealed 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：利用CD和二维 1 NMR监测酰胺质子交换，研究了溶于1％水的甘油中的鸡卵清溶菌酶。该蛋白的远紫外和近紫外CD光谱表明，甘油中溶菌酶的二级和三级结构与水中的相似。甘油中的溶菌酶热融解，随后CD光谱发生变化，表明三级结构展开，Tm为76.0±0.2°C，直到85°C，二级结构均无明显损失。这与在类似条件下在水中的Tm值分别为74.8±0.4°C和74.3±0.7°C的三级和二级结构的同时变性相反。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酰胺结构更好。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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