Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Molecular dynamics simulations provide a vehicle for capturing the structures, motions, and
interactions of biological macromolecules in full atomic detail. The accuracy of such …

Ion mobility mass spectrometry (IM-MS) allows the structural interrogation of biomolecules
by reporting their collision cross sections (CCSs). The major bottleneck for exploiting IM-MS …

Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …

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 …

Highlights•Classically, allostery induces a functional switch through a conformational
change.•Lately numerous studies concluded that allostery takes place through …

Large-scale conformational changes are essential to link protein structures with their
function at the cell and organism scale, but have been elusive both experimentally and …

Detailed descriptions of atomic coordinates and motions are required for an understanding
of protein dynamics and their relation to molecular recognition, catalytic function, and …