Maeda K, Rösch A, Maéda Y, Kalbitzer H R, Wittinghofer A
Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.
FEBS Lett. 1991 Apr 9;281(1-2):23-6. doi: 10.1016/0014-5793(91)80349-8.
We have expressed in E. coli segments of the rod portion of rabbit skeletal fast muscle myosin and compared physical properties of two different species, LMM-30 and LMM-30C'. LMM-30 consists of 263 amino acids including the original C-terminus of myosin heavy chain. LMM-30C' is colinear with LMM-30, but is devoid of 17 residues at the C-terminus. 1H NMR spectroscopy indicates that the C-terminus of LMM-30, but not of LMM-30C' is unfolded and freely mobile. Furthermore, the present results show that the unfolded C-terminus is essential for molecular assembly of LMM-30; at pH 8.0 LMM-30, but not LMM-30C', formed aggregates upon decreasing the ionic strength.
我们已在大肠杆菌中表达了兔骨骼肌快肌肌球蛋白杆状部分的片段，并比较了两种不同类型LMM-30和LMM-30C'的物理性质。LMM-30由263个氨基酸组成，包括肌球蛋白重链的原始C末端。LMM-30C'与LMM-30共线，但在C末端缺少17个残基。1H核磁共振光谱表明，LMM-30的C末端是未折叠且可自由移动的，而LMM-30C'的C末端并非如此。此外，目前的结果表明，未折叠的C末端对于LMM-30的分子组装至关重要；在pH 8.0时，降低离子强度后，LMM-30会形成聚集体，而LMM-30C'则不会。
