Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical
reactions are executed inside of biomolecular condensates formed by ultradynamic …

The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …

Pulse field gradient NMR methods have been used to determine the effective hydrodynamic
radii of a range of native and nonnative protein conformations. From these experimental …

Preparation of biological macromolecules in the pure state requires that cells be disrupted,
releasing and mixing the contents. Only the most stable and highly structured molecules can …

The paradigmatic disordered protein tau plays an important role in neuronal function and
neurodegenerative diseases. To disentangle the factors controlling the balance between …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

Protein folding and unfolding are coupled to a range of biological phenomena, from the
regulation of cellular activity to the onset of neurodegenerative diseases. Defining the nature …

15N relaxation dispersion experiments were applied to the isolated N-terminal SH3 domain
of the Drosophila protein drk (drkN SH3) to study microsecond to second time scale …

A sequence of seven alanine residues—too short to form an α-helix and whose side chains
do not interact with each other—is a particularly simple model for testing the common …

The ϕ, ψ backbone angle distribution of small homopolymeric model peptides is
investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study …