Robinson C V, Gross M, Eyles S J, Ewbank J J, Mayhew M, Hartl F U, Dobson C M, Radford S E
Dyson Perrins Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, UK.
Nature. 1994 Dec 15;372(6507):646-51. doi: 10.1038/372646a0.
The conformation of a three-disulphide derivative of bovine alpha-lactalbumin bound to the molecular chaperone GroEL has been investigated by monitoring directly its hydrogen exchange kinetics using electrospray ionization mass spectrometry. The bound protein is weakly protected from exchange to an extent closely similar to that of an uncomplexed molten globule state of the three-disulphide protein. Binding to GroEL in this system appears to involve relatively disordered partly folded states resembling intermediates formed in the very early stages of kinetic folding of many proteins in vitro.
通过使用电喷雾电离质谱法直接监测其氢交换动力学，研究了与分子伴侣GroEL结合的牛α-乳白蛋白三硫键衍生物的构象。结合的蛋白质从交换中受到的保护较弱，其程度与三硫键蛋白质未复合的熔融球状状态非常相似。在该系统中与GroEL的结合似乎涉及相对无序的部分折叠状态，类似于许多蛋白质在体外动力学折叠早期形成的中间体。
