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

What happens inside an enzyme's active site to allow slow and difficult chemical reactions to
occur so rapidly? This question has occupied biochemists' attention for a long time …

Nature has devised intrinsic electric fields (IEFs) that are engaged in electrostatic catalysis of
enzymes. But, how does the IEF target its function in enzymes that involve several reaction …

It is well-established that dynamics are central to protein function; their importance is
implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of …

Determining the interconverting conformations of dynamic proteins in atomic detail is a
major challenge for structural biology. Conformational heterogeneity in the active site of the …

Rational design and directed evolution have proved to be successful approaches to
increase catalytic efficiencies of both natural and artificial enzymes. Protein dynamics is …

Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing
how their structures and dynamics are closely intertwined to underlie their functions and …

Liquid–liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) and the
action of molecular chaperones are tightly connected. An important class of molecular …

Even after a century of investigation, our understanding of how enzymes work remains far
from complete. In particular, several factors that enable enzymes to achieve high catalytic …

Noncovalent interactions, in particular the hydrogen bonds and nonspecific long-range
electrostatic interactions are fundamental to biomolecular functions. A molecular …