| Mouse major urinary protein I (MUP-I) is an example of a mammalian pheromone-binding protein. Standard NMR techniques are used to study structural details of MUP-I in complex with a natural pheromone. NMR relaxation measurements are employed in mapping internal dynamics of free and pheromone-bound MUP-I. Analysis of data obtained at various temperatures are used to improve reliability of the measured values and to obtain additional information about dynamical and thermodynamical changes upon binding. The results are compared to molecular dynamic simulations. |
