Nanorheology of single protein molecules
نویسندگان
چکیده
The unfolding process of dimerized protein was investigated on a single protein basis using an atomic force microscope (AFM). In normal force-distance curve measurements, each monomer unit was unfolded step by step. We also measured the relax-stress response using “nanorheology AFM” that was newly developed to apply any required movements on a z-piezoelectric scanner, especially short stroke sinusoidal movements. This allowed us to investigate the dynamic response repeatedly without full stretching or rupturing. Although the protein molecule responded in-phase in most cases, we found a novel out-of-phase response around the stretching length where the second monomer unit unfolded. Simple calculation reproduced this phenomenon, which was attributed to the local refolding process.
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تاریخ انتشار 2001