Recent work has largely completed our understanding of the hydrogen-exchange chemistry
of unstructured proteins and nucleic acids. Some of the high-energy structural fluctuations …

This discussion, prepared for the Protein Society's symposium honoring the 100th
anniversary of Kaj Linderstrøm‐Lang, shows how hydrogen exchange approaches initially …

▪ Abstract In order to solve the immensely difficult protein-folding problem, it will be
necessary to characterize the barriers that slow folding and the intermediate structures that …

The rates at which hydrogens located at peptide amide linkages in proteins undergo isotopic
exchange when a protein is exposed to D2O depend on whether these amide hydrogens …

The hydrogen exchange (HX) rates of the slowest peptide group NH hydrogens in oxidized
cytochrome c (equine) are controlled by the transient global unfolding equilibrium. These …

A new statistical thermodynamic formalism has been developed in order to describe the
equilibrium folding pathway of proteins. The resulting formalism allows calculation of the …

Despite the general observation that single domain proteins denature in a completely
cooperative manner, amide hydrogen exchange of ribonuclease H in low levels of …

Background: Accessible surface area is a parameter that is widely used in analyses of
protein structure and stability. Accessible surface area does not, however, distinguish …

Two fundamentally different views of how proteins fold are now being debated. Do proteins
fold through multiple unpredictable routes directed only by the energetically downhill nature …

MA 02142, USA structure. In particular, the slowly exchanging amide protons in HP-35 have
protection factors that are slightly larger than those predicted if exchange occurred only from …