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

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

To promote the clinical theranostic performances of platinum‐based anticancer drugs,
imaging capability is urgently desired, and their chemotherapeutic efficacy needs to be …

Absorption of light by a molecule (donor, D) generates an excited state, which may
subsequently transfer the excitation to another chromophore (acceptor, A) in the vicinity …

Proteins are structurally dynamic macromolecules, and it is challenging to quantify the
conformational properties of their native state in solution. Nanopores can be efficient tools to …

The success of fluorescence experiments requires attention to experimental details and an
understanding of the instrumentation. There are also many potential artifacts that can distort …

The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …

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

Many eukaryotic proteins are disordered under physiological conditions, and fold into
ordered structures only on binding to their cellular targets. Such intrinsically disordered …

Fluorescence arguably constitutes the most widely used experimental approach in the field
of protein folding. Hence, any review of the use of fluorescence to probe protein stability and …