Conformation of bovine myelin basic protein purified with bound lipids
Conformation of bovine myelin basic protein purified with bound lipids
复制标题
用结合脂质纯化的牛髓磷脂碱性蛋白的构象
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
P. Cavatorta
中科院分区：
文献类型：
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作者：
E. Polverini;A. Fasano;F. Zito;P. Riccio;P. Cavatorta
髓鞘碱性蛋白（MBP）是髓鞘膜的一种外源性蛋白。其结构和功能尚不清楚。MBP以其水溶性形式被广泛研究，但它也以去污剂可溶的形式被已知，其用内源性髓鞘脂质纯化，并且应该对应于膜中蛋白质的天然形式。为了获得深入了解MBP的结构，我们进行了圆二色性（CD）实验的蛋白质在脂质自由和脂质结合的形式。我们的数据清楚地表明，无脂质的MBP主要是无序的，只有少量具有α-螺旋和β-折叠基序。另一方面，MBP的脂质结合形式似乎具有一致量的有序二级结构。理论预测，使用不同的计算方法，基本上证实了蛋白质的趋势，采取有序的二级结构，根据我们的CD结果。
Abstract The basic protein of myelin (called MBP) is an extrinsic protein of the myelin membrane. Its structure and function are still unknown. MBP has been extensively studied in its water-soluble form, but it is also known in a detergent-soluble form, which is purified with endogenous myelin lipids and should correspond to the native form of the protein in the membrane. In order to acquire insight into the structure of MBP, we have carried out circular dichroism (CD) experiments on the protein both in the lipid-free and in the lipid-bound form. Our data clearly show that lipid-free MBP is mainly disordered with only a small amount having α-helix and β-sheet motifs. On the other hand, the lipid-bound form of MBP appears to have a consistent amount of ordered secondary structure. Theoretical predictions, made using different computational methods, substantially confirm the tendency of the protein to assume an ordered secondary structure in accordance with our CD results.
影响因子：
5.6
作者：
KNELLER, DG;COHEN, FE;LANGRIDGE, R
通讯作者：
LANGRIDGE, R
小鼠髓磷脂 P2 蛋白基因的结构。
影响因子：
4.7
作者：
Narayanan,V;Kaestner,KH;Tennekoon,GI
通讯作者：
Tennekoon,GI
影响因子：
5.6
作者：
EISENBERG, D;SCHWARZ, E;WALL, R
通讯作者：
WALL, R