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 …

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 perspective reviews quantitative investigations of chemical exchange phenomena in
proteins and other biological macromolecules using NMR spectroscopy, particularly …

Time-dependent dynamical properties of molecules can be quantified with atomic resolution
by using solution-state NMR spectroscopy. A variety of NMR observables, including scalar …

A new NMR experiment is presented for the measurement of μs− ms time scale dynamics of
Asn and Gln side chains in proteins. Exchange contributions to the 15N line widths of side …

Although intermediates have long been recognised as fascinating species that form during
the folding of large proteins, the role that intermediates play in the folding of small, single …

Native molten globules are the most folded kind of intrinsically disordered proteins. Little is
known about the mechanism by which native molten globules bind to their cognate ligands …

NMR spin relaxation in the rotating frame (R 1ρ) is one of few methods available to
characterize chemical exchange kinetic processes occurring on μs− ms time scales. R 1ρ …

Conformational changes occurring on the microsecond− millisecond time scale in basic
pancreatic trypsin inhibitor (BPTI) are investigated using nuclear magnetic resonance …