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

Equilibrium simulations of molecular systems allow to extract many physicochemical
properties. Given an “accurate enough” model, a “large enough” simulation system and …

A longstanding goal in the field of intrinsically disordered proteins (IDPs) is to characterize
their structural heterogeneity and pinpoint the role of this heterogeneity in IDP function …

As the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus mutates,
finding effective drugs becomes more challenging. In this study, we use ultrasensitive …

Protein unfolding thermodynamic parameters are conventionally extracted from equilibrium
thermal and chemical denaturation experiments. Despite decades of work, the degree of …

Intrinsically disordered proteins (IDPs) contribute to a multitude of functions. De novo design
of IDPs should open the door to modulating functions and phenotypes controlled by these …

DNA-binding protein domains (DBDs) sample diverse conformations in equilibrium
facilitating the search and recognition of specific sites on DNA over millions of energetically …

Structural disorder in proteins is central to cellular signaling, where conformational plasticity
equips molecules to promiscuously interact with different partners. By engaging with multiple …

The relative magnitudes of noncovalent stabilization energies or the coupling free energies
in folded proteins are anisotropically distributed, uniquely influencing folding and functional …

We investigate the conformational properties of the intrinsically disordered DNA-binding
domain of CytR in the presence of the polymeric crowder polyethylene glycol (PEG) …