Stewart M, Roberts G C
J Mol Biol. 1983 May 15;166(2):219-25. doi: 10.1016/s0022-2836(83)80008-4.
The 1H nuclear magnetic resonance spectrum of alpha-tropomyosin contains a number of sharp peaks indicative of the presence of small regions of high flexibility in the molecule. Removal of 9 to 11 residues from the C-terminus by digestion with carboxypeptidase A causes a marked decline in the intensity of these peaks. The difference is consistent with at least the C-terminal four residues of the sequence (-Met-Thr-Ser-Ile) being highly mobile. The conformation of the C-terminus is thus radically different from the alpha-helical coiled-coil from which the bulk of the molecule is constructed.
α-原肌球蛋白的¹H核磁共振谱包含许多尖锐峰，这表明该分子中存在一些高柔韧性的小区域。用羧肽酶A消化从C末端去除9至11个残基会导致这些峰的强度显著下降。这种差异至少与序列的C末端四个残基（-Met-Thr-Ser-Ile）高度可移动是一致的。因此，C末端的构象与构成分子主体的α-螺旋卷曲螺旋截然不同。
