Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …

A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

Magic-angle spinning solid-state NMR spectroscopy is an important technique to study
molecular structure, dynamics and interactions, and is rapidly gaining importance in …

Molecular dynamics are essential for protein function. In some cases these dynamics involve
the interconversion between ground state, highly populated conformers and less populated …

The perspective reviews quantitative investigations of chemical exchange phenomena in
proteins and other biological macromolecules using NMR spectroscopy, particularly …

Although allostery draws increasing attention, not much is known about allosteric
mechanisms. Here we argue that in all proteins, allosteric signals transmit through multiple …

Allostery, the process by which distant sites within a protein system are energetically
coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely …

Gene-specific transcription factors (TFs) are key regulatory components of signaling
pathways, controlling, for example, cell growth, development, and stress responses. Their …

Most proteins consist of multiple domains. How do linkers efficiently transfer information
between sites that are on different domains to activate the protein? Mere flexibility only …

The three-dimensional structure of a protein is formed and maintained by the noncovalent
interactions among the amino-acid residues of the polypeptide chain. These interactions can …