Mendz G L, Brown L R, Martenson R E
Department of Biochemistry, University of Sydney, NSW, Australia.
Biochemistry. 1990 Mar 6;29(9):2304-11. doi: 10.1021/bi00461a014.
The interactions of myelin basic protein and peptides derived from it with detergent micelles of lysophosphatidylglycerol, lysophosphatidylserine, palmitoyllysophosphatidic acid, and sodium lauryl sulfate, and with mixed micelles of the neutral detergent dodecylphosphocholine and the negatively charged detergent palmitoyllysophosphatidic acid, were investigated by 1H NMR spectroscopy and circular dichroic spectropolarimetry. The results with single detergents suggested that there are discrete interaction sites in the protein molecule for neutral and anionic detergent micelles and that at least some of these sites are different for each type of detergent. The data on the binding of the protein and peptides to mixed detergent micelles suggested that intramolecular interactions in the intact protein and in one of the longer peptides limited the formation of helices and also that a balance between hydrophobic and ionic forces is achieved in the interactions of the peptides with the detergents. At high detergent/protein molar ratios, hydrophobic interactions appeared to be favored.
通过核磁共振氢谱（¹H NMR）和圆二色光谱偏振法研究了髓鞘碱性蛋白及其衍生肽与溶血磷脂酰甘油、溶血磷脂酰丝氨酸、棕榈酰溶血磷脂酸和十二烷基硫酸钠的去污剂胶束，以及与中性去污剂十二烷基磷酸胆碱和带负电荷的去污剂棕榈酰溶血磷脂酸的混合胶束之间的相互作用。单一去污剂的研究结果表明，蛋白质分子中存在中性和阴离子去污剂胶束的离散相互作用位点，并且每种类型的去污剂至少有一些位点是不同的。蛋白质和肽与混合去污剂胶束结合的数据表明，完整蛋白质和其中一种较长肽中的分子内相互作用限制了螺旋的形成，并且在肽与去污剂的相互作用中实现了疏水和离子力之间的平衡。在高去污剂/蛋白质摩尔比下，疏水相互作用似乎更受青睐。
