STRUCTURAL EFFECTS OF HYDRATION - STUDIES OF LYSOZYME BY C-13 SOLIDS NMR
STRUCTURAL EFFECTS OF HYDRATION - STUDIES OF LYSOZYME BY C-13 SOLIDS NMR
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DOI：
10.1002/bip.360291411
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发表时间：
1990-12-01
期刊：
影响因子：
2.9
通讯作者：
BRYANT, RG
中科院分区：
文献类型：
--
作者：
KENNEDY, SD;BRYANT, RG
本文报道了用静态和魔角旋转交叉极化法在50.3MHz下获得的溶菌酶在几种含水量下的~（13）C-NMR谱。与冻干蛋白质相比，水合材料中的线宽和随后的分辨率得到了显著改善。线变窄是不相称的质子-碳偶极-偶极耦合的损失或显着变化的弛豫参数表征从质子到碳的Hartmann-Hahn交叉极化实验中的磁化转移。我们解释这些数据的水引起的蛋白质采样的局部构象的分布减少，虽然占数据所需的构象重定向的幅度不一定很大，也不意味着一个主要的展开的蛋白质脱水。
13C-nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic-angle-spinning-cross polarization nethods are reported at several water contents. The line widths and consequent resolution in the hydrated material is substantially improved over that in the lyophilized protein. The line narrowing is not commensurate with loss of a proton-carbon dipole-dipole coupling or dramatic changes in the relaxation parameters characterizing magnetization transfer from protons to carbon in the Hartmann-Hahn cross-polarization experiment. We interpret these data in terms of the water inducing a decrease in the distribution of local conformations sampled by the protein, although the magnitude of the conformational reorientations required to account for the data are not necessarily large nor do they imply a major unfolding of the protein on dehydration.