Real-time NMR study of protein transient states

Identification and characterization of a monomer-dimer exchange process in the excited state of b2 microglobulin by a combination of real-time NMR and CPMG relaxation-dispersion NMR. This conformational state has been previously shown in our team to be 7 times more prone to aggregation than the native state.
Collaborations: A.Corazza, G. Esposito (Univ. of Udine, Italy); V. Forge (iRTSV, CEA Grenoble, France)