Objective
An important goal in protein dynamics is to get a satisfactory description of the conformational landscape of the active sites in proteins. A growing set of experimental data confirms the existence, inside a main structural protein state, of different substrates, whose conformation is expected to control the ligand binding kinetics, depending on several factors, as protein sequence, solvent, pH, temperature. The problem is to find conformations that are relevant for function. Hence the use of a local probe for the active sites, like X-ray absorption spectroscopy, which seems to be of great help in looking specifically at the important protein conformations.
The study of the temperature dependence of the thermal (Debye-Waller) and structural (bond lengths and bond angles) parameters in the active site structure of oxygen binding proteins by using X-ray absorption spectroscopy will allow the probing of important conformational substrates in the protein. Simultaneous laser excitation will provide the possibility of studying the dynamic time evolution of reversible ligand binding processes as a function of temperature, making it possible to probe intermediate states. A report on the dynamics of the protein active site by temperature dependent X-ray absorption spectroscopy will therefore provide new information on the still confused conformational landscape problem of oxygen-binding proteins.
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67100 L'Aquila
Italy