Single-molecule fluorescence resonance energy transfer (smFRET) is one of the most
general and adaptable single-molecule techniques. Despite the explosive growth in the …

BACKGROUND Biomolecular mechanisms are typically inferred from static structural
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …

Ever since their introduction two decades ago, single-molecule (SM) fluorescence methods
have matured and branched out to address numerous biological questions, which were …

A complete understanding of a protein-folding mechanism requires description of the
distribution of microscopic pathways that connect the folded and unfolded states. This …

Optical imaging and analysis of single molecules continue to unfold as powerful ways to
study the individual behavior of biological systems, unobscured by ensemble averaging …

Methods for chemical modifications of proteins have been crucial for the advancement of
proteomics. In particular, site-specific covalent labeling of proteins with fluorophores and …

Fluorescence microscopy and spectroscopy data hold a wealth of information on the
investigated molecules, structures, or organisms. Nowadays, the same fluorescence data set …

Single-molecule FRET (smFRET) has become a mainstream technique for studying
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …

Single-molecule methods have matured into powerful and popular tools to probe the
complex behaviour of biological molecules, due to their unique abilities to probe molecular …

Fluorescence resonance energy transfer (FRET) represents a mechanism to transport light
energy at the nanoscale, as exemplified by nature's light-harvesting complexes. Here we …