Fung L W, Lu H Z, Hjelm R P, Johnson M E
FEBS Lett. 1986 Mar 3;197(1-2):234-8. doi: 10.1016/0014-5793(86)80333-7.
Human erythrocyte spectrin molecules exhibit relatively sharp (30-50 Hz) proton NMR signals in the aliphatic region. A standard solvent presaturation pulse sequence that also partially suppresses the broad envelope from protons with rigid structures in spectrin and selectively enhances the sharp resonances has been used to characterize the behavior of these resonances. The overall resonance pattern strongly resembles that of the denatured spectrin. The observed spectra are also quite similar to the line-broadened spectrum from a mixture of amino acids that corresponds to the composition of the spectrin molecule. These data indicate the existence of regions exhibiting rapid internal motions within the intact spectrin molecule, and suggest that the amino acid composition of the residues giving rise to the sharp resonances is quite similar to that of the full spectrin molecule.
人红细胞血影蛋白分子在脂肪族区域呈现出相对尖锐（30 - 50赫兹）的质子核磁共振信号。一种标准的溶剂预饱和脉冲序列，它还能部分抑制血影蛋白中具有刚性结构的质子产生的宽峰包络，并选择性增强尖锐的共振信号，已被用于表征这些共振信号的行为。整体共振模式与变性血影蛋白的模式极为相似。观察到的光谱也与对应血影蛋白分子组成的氨基酸混合物的谱线展宽光谱非常相似。这些数据表明完整血影蛋白分子内存在呈现快速内部运动的区域，并表明产生尖锐共振信号的残基的氨基酸组成与完整血影蛋白分子的氨基酸组成相当相似。
