Optical tweezers have become the method of choice in single-molecule manipulation
studies. In this Primer, we first review the physical principles of optical tweezers and the …

Manipulation of individual molecules with optical tweezers provides a powerful means of
interrogating the structure and folding of proteins. Mechanical force is not only a relevant …

Single-molecule measurements have greatly enhanced our understanding of living systems.
Biological systems offer nanopores, a sub-class of membrane proteins, the well-defined …

We present simple considerations of how differences in time scales of motions of protons,
the lightest and fastest chemical moiety, and the much longer time scales associated with …

Correct folding is a prerequisite for the biological activity of most proteins. Folding has
largely been studied using in vitro refolding assays with isolated small, robustly folding …

In vivo, proteins fold and function in a complex environment subject to many stresses that
can modulate a protein's energy landscape. One aspect of the environment pertinent to …

We report on the use of atomic force microscopy (AFM) to identify and characterize an
intermediate state in macrocycle shuttling in a hydrogen bonded amide-based molecular …

Optical tweezers has emerged as a powerful tool to study folding, ligand binding, and motor
enzymes. The manipulation of proteins with optical tweezers requires attaching molecular …

The link between cofactor binding and protein activity is well-established. However, how
cofactor interactions modulate folding of large proteins remains unknown. We use optical …

Osmolytes are well known to protect the protein structure against different chemical and
physical denaturants. Since their actions with protein surfaces are mechanistically …