Atomic force microscopy (AFM) has proved to be an essential tool of structural biology, being able not only to image but also to manipulate single biological molecules. These techniques make it possible to investigate the nanometer scale structure of single biological macromolecules and to study how an external force drives single biological molecules towards nonequilibrium conformations, by stretching and breaking bonds and interactions. This chapter focuses on the capabilities of the AFM-based single molecule methodologies to bring us into the nanometer-scale world of the single DNA molecules and into the pico-Newton force-scales of the interactions that sustain the protein folding.
Inside the small length and energy scales of the world of the individual biological molecule
Zuccheri G;
2005
Abstract
Atomic force microscopy (AFM) has proved to be an essential tool of structural biology, being able not only to image but also to manipulate single biological molecules. These techniques make it possible to investigate the nanometer scale structure of single biological macromolecules and to study how an external force drives single biological molecules towards nonequilibrium conformations, by stretching and breaking bonds and interactions. This chapter focuses on the capabilities of the AFM-based single molecule methodologies to bring us into the nanometer-scale world of the single DNA molecules and into the pico-Newton force-scales of the interactions that sustain the protein folding.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
