Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering
Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering
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DOI：
10.1016/s0022-2836(02)00566-1
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发表时间：
2002-08-02
影响因子：
5.6
通讯作者：
Kuwajima, K
中科院分区：
文献类型：
--
作者：
Arai, M;Ito, K;Kuwajima, K
为了监测蛋白质折叠过程中的快速压缩过程，我们使用了停流小角度X射线散射技术与基于二维电荷耦合器件的X射线探测器相结合，可以显着提高数据的信噪比，并测量了α-乳清蛋白的动力学重折叠反应。结果清楚地表明，α-乳清蛋白的动力学折叠中间体的回转半径和整体形状与平衡时观察到的熔球状态相同。因此，动力学折叠中间体和平衡熔球状态之间的一致性被牢固地确立。目前的结果还表明，折叠中间体比天然状态更加水合，并且在从熔球到天然状态的转变过程中形成特定侧链堆积时，水合水分子会脱水。 (C) 2002 年，爱思唯尔科学有限公司出版。
To monitor the fast compaction process during protein folding, we have used a stopped-flow small-angle X-ray scattering technique combined with a two-dimensional charge-coupled device-based X-ray detector that makes it possible to improve the signal-to-noise ratio of data dramatically, and measured the kinetic refolding reaction of alpha-lactalbumin. The results clearly show that the radius of gyration and the overall shape of the kinetic folding intermediate of alpha-lactalbumin are the same as those of the molten globule state observed at equilibrium. Thus, the identity between the kinetic folding intermediate and the equilibrium molten globule state is firmly established. The present results also suggest that the folding intermediate is more hydrated than the native state and that the hydrated water molecules are dehydrated when specific side-chain packing is formed during the change from the molten globule to the native state. (C) 2002 Published by Elsevier Science Ltd.