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Effect Of Hydrostatic Pressure On Fluorescence Reactions In Proteins

°The effect of hydrostatic pressure (0-2.6 kbar) on the acrylamide quenching of several single tryptophan containing proteins has been studied using phase fluorescence lifetime measurements, at 25C. For the model system, N-acetyl-L-tryptophanamide in water, we find essentially no dependence of the quenching rate constant, kq, on pressure. For the internal tryptophan residues of ribonuclease T1 and cod parvalbumin, we also find essentially no pressure dependence for the acrylamide kq. The low apparent activation volumes, LW*, characterize these quenching processes as involving very small amplitude fluctuations in the protein structures. Only for a poised monomer ↔tetramer equilibrium of melittin were we able to observe a significant effect of pressure on kq and this is due to the pressure induced shift in the equilibrium position.