Abstract

Atomic force microscopy (AFM) has become a common tool for biophysical studies of proteins; mainly due its property to perform characterizations near physiological conditions. The tertiary and quaternary structures, forces driving folding-unfolding processes, and secondary structure elements can be studied in their native environments allowing high resolution level associated with small distortions. This review outlines the operational principles and applications of AFM for protein biophysics.

Keywords: atomic force microscopy, afm, force spectroscopy, protein, protein adsorption