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Abstract: NMR is a powerful tool for characterizing the structure and dynamics of proteins at the site‐specific level. A variety of NMR techniques can be applied to study various conformational states during the folding process, including the highly unfolded, partially folded, and native states. One particularly powerful method is the combination of NMR with hydrogen–deuterium exchange to indicate the formation of hydrogen bonds in proteins. Examples of the application of a variety of NMR methods to the protein folding studies of α‐lactalbumin and c‐type lysozyme are presented. [Copyright &y& Elsevier]