Proton NMR studies of denatured lysozyme.

Evidence is presented from 1H NMR studies for non-random conformational behaviour in denatured lysozyme in aqueous solution. A method is presented which permits the assignment of resonances in the 1H NMR spectrum of the denatured protein by observing magnetisation transfer from resonances of the native state. The use of these experiments in characterising the denatured state and the significance of these studies for the investigation of protein folding are discussed.