SEM Imaging of Single Heavy Meromyosin Molecules on Hydrophilic Silicon Surface

抄録

The fine structure of skeletal muscle heavy meromyosin (HMM) with two heads connected to a thin tail was clearly imaged with a high-resolution scanning electron microscope (SEM) by negative staining on a hydrophilic silicon surface. The single molecular image of HMM was analyzed. A structural change in the HMM head on binding of adenosine triphosphate (ATP) was detected. The HMM molecules with head(s) bent at 6-8 nm from the head-tail junction directed toward the end of the tail were found frequently in the presence of ATP. The estimated value for the bending angle was about 20° on average.