Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

Although it is now relatively well understood how sequence defines and impacts global
protein stability in specific structural contexts, the question of how sequence modulates the …

The synthetic neomycin‐sensing riboswitch interacts with its cognate ligand neomycin as
well as with the related antibiotics ribostamycin and paromomycin. Binding of these …

The phenomenon of chemical or conformational exchange in NMR spectroscopy has
enabled detailed characterization of time-dependent aspects of biomolecular function …

Although many proteins possess a distinct folded structure lying at a minimum in a funneled
free energy landscape, thermal energy causes any protein to continuously access lowly …

Protein folding is a highly complex process proceeding through a number of disordered and
partially folded nonnative states with various degrees of structural organization. These …

Pressure and temperature are the two fundamental variables of thermodynamics.
Temperature and chemical perturbation are central experimental tools for the exploration of …

Most proteins are highly flexible and can adopt conformations that deviate from the
energetically most favorable ground state. Structural information on these lowly populated …

Molecular dynamics play a significant role in how molecules perform their function. A critical
method that provides information on dynamics, at the atomic level, is NMR-based relaxation …

Protein conformational landscapes define their functional properties as well as their
proteostasis. Hence, detailed mapping of these landscapes is necessary to understand and …