Ontology highlight
ABSTRACT:
SUBMITTER: Van Patten WJ
PROVIDER: S-EPMC5760306 | biostudies-other | 2018 Jan
REPOSITORIES: biostudies-other
Chemphyschem : a European journal of chemical physics and physical chemistry 20171204 1
Quantifying the energy landscape underlying protein-ligand interactions leads to an enhanced understanding of molecular recognition. A powerful yet accessible single-molecule technique is atomic force microscopy (AFM)-based force spectroscopy, which generally yields the zero-force dissociation rate constant (k<sub>off</sub> ) and the distance to the transition state (Δx<sup>≠</sup> ). Here, we introduce an enhanced AFM assay and apply it to probe the computationally designed protein DIG10.3 bind ...[more]