Andreani C, Filabozzi A, Menzinger F, Desideri A, Deriu A, Di Cola D
Dipartimento di Fisica, Università di Roma Tor Vergata, Italy.
Biophys J. 1995 Jun;68(6):2519-23. doi: 10.1016/S0006-3495(95)80434-0.
The low energy dynamic of the enzyme Cu,Zn superoxide dismutase have been investigated by means of quasielastic neutron scattering in the temperature range 4-320 K. Below 200 K the scattering is purely elastic, while above this temperature a pronounced decrease in the elastic intensity is observed, together with the onset of a small quasielastic component. This behavior is similar to that previously observed in other more flexible globular proteins, and can be attributed to transitions between slightly different conformational substates of the protein tertiary structure. The presence of only a small quasielastic component, whose intensity is < or = 25% of the total spectrum, is related to the high structural rigidity of this protein.
通过在4 - 320 K温度范围内的准弹性中子散射研究了铜锌超氧化物歧化酶的低能动力学。在200 K以下,散射是纯弹性的,而高于此温度时,观察到弹性强度明显下降,同时出现一个小的准弹性分量。这种行为与先前在其他更灵活的球状蛋白质中观察到的行为相似,并且可归因于蛋白质三级结构的略有不同构象亚态之间的转变。仅存在一个小的准弹性分量,其强度小于或等于总光谱的25%,这与该蛋白质的高结构刚性有关。