Hydrogen exchange techniques, with their residue-level specificity, ex
quisite sensitivity, and adaptability to many solution conditions, are
becoming essential to the study of protein stability, folding and dyn
amics. Recent studies have elucidated the structures of intermediates
formed transiently during protein folding and rare partially folded en
sembles present at equilibrium. Analysis of hydrogen exchange mechanis
ms has revealed protein stability and kinetics at the level of individ
ual residues. (C) Current Biology Ltd ISSN 0958-1669.