The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells is the result of cycles of mechano-sensing, mechano-transduction, and mechano-response. Recently developed single-molecule atomic force microscopy (AFM) techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins, such as titin (an elastic mechano-sensing protein found in muscle) and polycystin-1 (PC1, a mechanosensor found in the kidney).
- ASME Nanotechnology Council
Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1
- Views Icon Views
- Share Icon Share
- Search Site
Ma, L, Xu, M, & Oberhauser, AF. "Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1." Proceedings of the ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. Houston, Texas, USA. February 7–10, 2010. pp. 365-366. ASME. https://doi.org/10.1115/NEMB2010-13093
Download citation file: