Fang J K, Jacobs J W, Kanner B I, Racker E, Bradshaw R A
Proc Natl Acad Sci U S A. 1984 Nov;81(21):6603-7. doi: 10.1073/pnas.81.21.6603.
The amino acid sequence of bovine heart mitochondrial coupling factor 6 (F6) has been determined by automated Edman degradation of the whole protein and derived peptides. Preparations based on heat precipitation and ethanol extraction showed allotypic variation at three positions while material further purified by HPLC yielded only one sequence that also differed by a Phe-Thr replacement at residue 62. The mature protein contains 76 amino acids with a calculated molecular weight of 9006 and a pI of approximately equal to 5, in good agreement with experimentally measured values. The charged amino acids are mainly clustered at the termini and in one section in the middle; these three polar segments are separated by two segments relatively rich in nonpolar residues. Chou-Fasman analysis suggests three stretches of alpha-helix coinciding (or within) the high-charge-density sequences with a single beta-turn at the first polar-nonpolar junction. Comparison of the F6 sequence with those of other proteins did not reveal any homologous structures.
通过对完整蛋白质及其衍生肽段进行自动埃德曼降解,已确定了牛心线粒体偶联因子6(F6)的氨基酸序列。基于热沉淀和乙醇提取的制剂在三个位置显示出同种异型变异,而通过高效液相色谱进一步纯化的材料仅产生了一种序列,该序列在第62位残基处也存在苯丙氨酸 - 苏氨酸替换差异。成熟蛋白含有76个氨基酸,计算分子量为9006,pI约等于5,与实验测量值吻合良好。带电荷的氨基酸主要聚集在末端和中间的一个区域;这三个极性片段被两个相对富含非极性残基的片段隔开。周 - 法斯曼分析表明,有三段α螺旋与高电荷密度序列重合(或在其范围内),在第一个极性 - 非极性交界处有一个单一的β转角。将F6序列与其他蛋白质的序列进行比较,未发现任何同源结构。