Protein dynamics by NMR has been reviewed extensively in recent years [1–10]. These
surveys show decisively that information on structure should be complemented by …

Molecular recognition by proteins is fundamental to molecular biology. Dissection of the
thermodynamic energy terms governing protein–ligand interactions has proven difficult, with …

By means of atomistic molecular dynamics simulations we investigate the behaviour of poly
(N-isopropylacrylamide), PNIPAM, in water at temperatures below and above the lower …

Molecular dynamics (MD) simulation is a powerful tool for exploring the conformational
energy landscape of proteins, and the reliability of MD results is crucially dependent on the …

Dynamic processes are responsible for the functionality of a range of materials,
biomolecules, and catalysts. We report a detailed systematic study of the modulation of …

In DNP MAS NMR experiments at∼ 80–110 K, the structurally important− 13CH3 and−
15NH3+ signals in MAS spectra of biological samples disappear due to the interference of …

The large majority of three-dimensional structures of biological macromolecules have been
determined by X-ray diffraction of crystalline samples. High-resolution structure …

In this paper, we seek to compare the internal dynamics of a small globular protein, SH3
domain from α-spectrin, in solution and in a crystalline state. The comparison involves side …

Despite their importance in macromolecular interactions and functions, the dynamics of
lysine side-chain amino groups in proteins are not well understood. In this study, we have …

Motions of proteins are essential for the performance of their functions. Aliphatic protein side
chains and their motions play critical roles in protein interactions: for recognition and binding …