Dunker A K, Williams R W, Gaber B P, Peticolas W L
Biochim Biophys Acta. 1979 May 17;553(2):351-7. doi: 10.1016/0005-2736(79)90238-4.
Complexes of the B-protein of fd phage with the model lipid dipalmitoyl phosphatidylcholine (DPPC) were made by sonication of the fd phage in the presence of dipalmitoyl phosphatidylcholine. Both laser Raman spectra and circular dichroism show the protein in the membrane to be almost entirely in the beta-sheet conformation. This beta-sheet conformation is found to be independent of the temperature between 10 degrees C and 50 degrees C. On the other hand, the protein has a very dramatic effect on the organization of the lipid bilayer. An aqueous dispersion of 1 : 1 lipid/protein mixture gives a broad conformational transition of DPPC which occurs between 10 degrees C and 30 degrees C. This contrasts markedly with simple aqueous DPPC dispersions which show a sharp transition at 41 degrees C. This appears to be the first reported example of the lowering of the conformational transition of a membrane bilayer by an intrinsic membrane protein.
通过在二棕榈酰磷脂酰胆碱（DPPC）存在的情况下对fd噬菌体进行超声处理，制备了fd噬菌体的B蛋白与模型脂质二棕榈酰磷脂酰胆碱（DPPC）的复合物。激光拉曼光谱和圆二色性均表明，膜中的蛋白质几乎完全处于β-折叠构象。发现这种β-折叠构象在10℃至50℃之间与温度无关。另一方面，该蛋白质对脂质双层的组织有非常显著的影响。1:1脂质/蛋白质混合物的水分散体使DPPC发生宽泛的构象转变，该转变发生在10℃至30℃之间。这与简单的DPPC水分散体形成鲜明对比，后者在41℃时显示出尖锐的转变。这似乎是首次报道的内在膜蛋白降低膜双层构象转变温度的例子。
