The term B-factor, sometimes called the Debye–Waller factor, temperature factor, or atomic
displacement parameter, is used in protein crystallography to describe the attenuation of X …

Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

Dramatic advances in protein structure prediction have sparked debate as to whether the
problem of predicting structure from sequence is solved or not. Here, I argue that AlphaFold2 …

The discovery of small-molecule inhibitors requires suitable binding pockets on protein
surfaces. Proteins that lack this feature are considered undruggable and require innovative …

Allostery is the process by which biological macromolecules (mostly proteins) transmit the
effect of binding at one site to another, often distal, functional site, allowing for regulation of …

Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for
analyzing protein structure, interaction, and dynamics at atomic resolution and in various …

Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Enzymes must be ordered to allow the stabilization of transition states by their active sites,
yet dynamic enough to adopt alternative conformations suited to other steps in their catalytic …

The enzyme soybean lipoxygenase (SLO) provides a prototype for deep tunneling
mechanisms in hydrogen transfer catalysis. This work combines room temperature X-ray …