An NMR approach is presented that provides detailed information about short-lived, transient interactions between protein molecules in solution. The approach is based on the longitudinal paramagnetic relaxation rates of the protein nuclei and requires that at least one of the interacting molecules is paramagnetic. The specific interactions are monitored by the intermolecular paramagnetic contribution to the relaxation of protons at or close to the interaction surface. By applying the approach to plastocyanin from Anabaena variabilis, specific regions of interaction that may be involved in the electron self-exchange process of this plastocyanin were identified. This is in accord with recent 15N NMR relaxation studies of the backbone dynamics of Anabaena variabilis plastocyanin, with site-directed mutagenesis studies of the functional importance of the corresponding regions in Phormidium laminosum plastocyanin and with the crystal packing surface of P. laminosum plastocyanin.