Low energy dynamics of globular proteins studied by inelastic neutron scattering
Low energy dynamics of globular proteins studied by inelastic neutron scattering
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DOI：
10.1016/s0022-3697(99)00103-1
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发表时间：
1999-08-01
影响因子：
4
通讯作者：
Shibata, K
中科院分区：
文献类型：
--
作者：
Kataoka, M;Kamikubo, H;Shibata, K
为了揭示折叠蛋白质特有的动力学性质，对折叠的和未折叠的葡萄球菌核酸酶以及肌红蛋白在100K和300K下进行了非弹性中子散射测量，在100K观察到的这三种蛋白质的S(Q，omega)基本上是相同的。在低温下的低能动态中没有表现出蛋白质的个体性。低能激发峰的位置随分子量的变化而变化，表明激发是由整个分子的模式引起的。在300K下观察到折叠时动力学性质的变化，表明非简谐运动是功能所必需的。(C)1999由爱思唯尔科学有限公司出版。版权所有。
In order to reveal the dynamical properties specific to the folded protein, inelastic neutron scattering measurements were performed for the folded and the unfolded Staphylococcal nuclease, and myoglobin at 100 K and 300 K. The observed S(Q, omega) at 100 K for these three were essentially identical. Protein individuality was not expressed in the low energy dynamics at low temperature. The peak position of low energy excitation showed molecular weight dependence, suggesting that the excitation is originated from modes extended over a whole molecule. The changes in dynamical properties upon folding were observed at 300 K, suggesting that anharmonic motion is essential for function. (C) 1999 Published by Elsevier Science Ltd. All rights reserved.