INSIGHTS INTO PROTEIN-FOLDING FROM NMR

NMR has emerged as an important tool for studies of protein folding be cause of the unique structural insights it can provide into many aspec ts of the folding process. Applications include measurements of kineti c folding events and structural characterization of folding intermedia tes, partly folded states, and unfolded states. Kinetic information on a time scale of milliseconds or longer can be obtained by real-time N MR experiments and by quench-flow hydrogen-exchange pulse labeling. Al though NMR cannot provide direct information on the very rapid process es occurring during the earliest stages of protein folding, studies of isolated peptide fragments provide insights into likely protein foldi ng initiation events. Multidimensional NMR techniques are providing ne w information on the structure and dynamics of protein folding interme diates and both partly folded and unfolded states.