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

The cellular interior is composed of a variety of microenvironments defined by distinct local
compositions and composition-dependent intermolecular interactions. We review the …

The effects of crowding in biological environments on biomolecular structure, dynamics, and
function remain not well understood. Computer simulations of atomistic models of …

The cytoplasm is a crowded, visco-elastic environment whose physical properties change
according to physiological or developmental states. How the physical properties of the …

Abstract Effects of macromolecular crowding on structural and functional properties of
ordered proteins, their folding, interactability, and aggregation are well documented. Much …

Liquid–liquid phase separation (LLPS) plays an important role in a variety of biological
processes and is also associated with protein aggregation in neurodegenerative diseases …

Four types of environmental effects that can affect macromolecular reactions in a living cell
are defined: nonspecific intermolecular interactions, side reactions, partitioning between …

The proper functioning of any protein depends on its three dimensional conformation which
is achieved by the accurate folding mechanism. Keeping away from the exposed stress …

Knowledge of the Michaelis–Menten parameters and their meaning in different
circumstances is an essential prerequisite to understanding enzyme function and behaviour …

Investigating protein–protein interactions is crucial for understanding cellular biological
processes because proteins often function within molecular complexes rather than in …