Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

Protein function depends on transitions from the ground state to higher energy states.
Deviations from the ground-state structure result from chemical reactivity and conformational …

The solution properties, including hydrodynamic quantities and the radius of gyration, of
globular proteins are calculated from their detailed, atomic-level structure, using bead …

Biological molecules are often highly dynamic, and this flexibility can be critical for function.
The large range of sampled timescales and the fact that many of the conformers that are …

Molecular dynamics are essential for protein function. In some cases these dynamics involve
the interconversion between ground state, highly populated conformers and less populated …

The heteronuclear NMR relaxation of globular proteins depends on the anisotropic
rotational diffusion tensor. Using our previous developments for prediction of hydrodynamic …

Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …

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 …

Site-directed spin labeling is a general method for investigating structure and conformational
switching in soluble and membrane proteins. It will also be an important tool for exploring …