▪ 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 …

A thermodynamically and kinetically simple picture of protein folding envisages only two
states, native (N) and unfolded (U), separated by a single activation free energy barrier, and …

Analysis of the kinetics of hydrogen exchange in biological macromolecules is a powerful
method for studying both their structural and dynamic properties. This arises from our …

Measuring protein conformational stability is one key to solving the protein folding problem.
The conformational stability is the free energy change of the unfolding reaction, F↔ U, under …

Experiments were done to study the dynamic structural motions that determine protein
hydrogen exchange (HX) behavior. The replacement of a solvent‐exposed lysine residue …

Direct structural information obtained for many proteins supports the following conclusions.
The amino acid sequences of proteins can stabilize not only the final native state but also a …

Native-state hydrogen exchange experiments under EX1 conditions can distinguish partially
unfolded intermediates by their formation rates and identify the amide hydrogens exposed …

We have used native state exchange to examine the energy landscape of the well-
characterized protein T4 lysozyme. Although the protein exhibits two-state behavior by …

Measuring the conformational stability of a protein is one key to solving the protein folding
problem. It is also of practical importance for answering questions such as these: 1. How …

Hydrogen-deuterium exchange (HDX) measured by nuclear magnetic resonance (NMR)
provides structural information for proteins relating to solvent accessibility and flexibility …