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首页> 外文期刊>Journal of Biotechnology >Protein folding and stability investigated by fluorescence, circulardichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: theflavodoxin story
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Protein folding and stability investigated by fluorescence, circulardichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: theflavodoxin story

机译：通过荧光，圆二色性（CD）和核磁共振（NMR）光谱研究蛋白质折叠和稳定性：黄酮毒素的故事

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In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introduced. These techniques are: circular dichroism (CD) spectroscopy, fluorescence emission spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy in combination with the hydrogen exchange methodology. Results on the denaturant-induced and thermal equilibrium unfolding of apoflavodoxin from A. vinelandii, i.e. flavodoxin in the absence of the riboflavin-5'-monophosphate (FMN) cofactor, are discussed. A scheme for the equilibrium unfolding of apoflavodoxin is presented which involves a relatively stable molten globule-like intermediate. Denaturant-induced apoflavodoxin (un)folding as followed at the residue-level by NMR shows that the transition of native A. vinelandii apoflavodoxin to its molten globule state is highly co-operative. However, the unfolding of the molten globule to the unfolded state of the protein is non-co-operative. A comparison of the folding of A. vinelandii flavodoxin with the folding of flavodoxin from Anabaena PCC 7119 is made. The local stabilities of apo- and holoflavodoxin from A. vinelandii as measured by NMR spectroscopy are compared. Both Che Y and cutinase, which have no sequence homology with apoflavodoxin but which share the flavodoxin-like topology, have stabilisation centres different from that of apoflavodoxin from A. vinelandii. The stable centres of structurally similar proteins can thus reside in different parts of the same protein topology. Insight in the variations in (local) unfolding processes of structurally similar proteins can be used to stabilise proteins with a flavodoxin-like fold. Finally, the importance of some recent experimental and theoretical developments for the study of flavodoxin folding is briefly discussed.
机译：在这篇综述中，总结了关于葡萄固氮菌黄酮毒素的折叠和稳定性的实验结果。通过这样做，简要介绍了用于研究蛋白质折叠和稳定性的三种主要光谱技术。这些技术是：圆二色性（CD）光谱，荧光发射光谱和核磁共振（NMR）光谱结合氢交换方法。讨论了在不存在核黄素5'-单磷酸酯（FMN）辅因子的情况下，来自葡萄球菌的载黄酮毒素（即黄酮毒素）的变性诱导和热平衡解开的结果。提出了载脂蛋白黄平衡平衡展开的方案，该方案涉及相对稳定的熔融小球状中间体。变性剂诱导的载脂蛋白毒素（un）折叠，然后通过NMR在残基水平上显示，天然的A. vinelandii载脂蛋白毒素向其熔融小球状态的转变是高度合作的。但是，将熔融小球展开至蛋白质的展开状态是不合作的。比较了A. vinelandii黄酮毒素的折叠与来自Anabaena PCC 7119的黄素毒素的折叠。比较了核磁共振波谱法测定的A. vinelandii载脂蛋白和全黄酮毒素的局部稳定性。 Che Y和角质酶均与载黄酮毒素没有序列同源性，但共有类黄酮毒素的拓扑结构，其稳定中心不同于A. vinelandii的载黄素毒素。因此，结构相似的蛋白质的稳定中心可以位于同一蛋白质拓扑的不同部分。结构相似蛋白在（局部）展开过程中变化的见解可用于稳定具有黄素类毒素折叠的蛋白。最后，简要讨论了一些最近的实验和理论发展对黄酮毒素折叠研究的重要性。

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