In-cell structural biology aims at extracting structural information about proteins or nucleic
acids in their native, cellular environment. This emerging field holds great promise and is …

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

A detailed knowledge of the complex processes that make cells and organisms alive is
fundamental in order to understand diseases and to develop novel drugs and therapeutic …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

NMR spectroscopy has been applied to cells and tissues analysis since its beginnings, as
early as 1950. We have attempted to gather here in a didactic fashion the broad diversity of …

Macromolecular crowding is known to affect protein folding, binding of small molecules,
interaction with nucleic acids, enzymatic activity, protein-protein interactions, and protein …

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

Classical structural biology approaches allow structural characterization of biological
macromolecules in vitro, far from their physiological context. Nowadays, thanks to the wealth …

How proteins sense and navigate the cellular interior to find their functional partners remains
poorly understood. An intriguing aspect of this search is that it relies on diffusive encounters …

Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing
essential roles in all aspects of cellular and extracellular biochemistry. To understand their …