ABSTRACT
The interaction of proteins with the nucleic acids, DNA and RNA, is fundamental for many processes in life. For example, proteins that bind to speci¡c DNA target sequences control processes of transcription, translation, and regulation of genes. Small ligands whose binding af¡nity to DNA has little or no sequence-speci¡city are often able to interfere with those processes and are thus commonly used as anticancer drugs and antibiotics. On the other hand, ligands whose binding af¡nity to RNA is sequence-speci¡c are able to interfere with post-transcriptional processes like splicing. Atomic force microscopy (AFM)-based single molecule force spectroscopy (SMFS) enables the study of such binding processes, illuminating the mechanism, kinetics, binding speci¡city, and the underlying energy.
