Here we present a method for exploring proteins dynamics while revealing a significant number of its quantitative properties including its diffusion coefficient, bound and free fraction, protein concentration and binding-unbinding kinetics. The method is based on the combination of live-cell imaging modalities combined onto a single experiment that we term time-resolved continuous photobleaching (TRIP). By applying the method on structural proteins in the nucleus, we demonstrate the complex function of lamin A that is of crucial important for maintaining the genome organization in the nucleus.