Pressure-induced Critical Association of Myoglobin
Oligomeric proteins generally tend to dissociate under pressure, while aggregation is often observed in the pressure-denatured state. We report on a pressure-induced association of native myoglobin in the low-pressure regime. Depending on solvent conditions, the monomer becomes unstable above a critical pressure. The association process involves an initial lag phase due to seed formation, an intermediate reversible oligomeric state and a final structurally altered precipitate. Using static and dynamic light scattering, we discuss the kinetics of association, the effect of pH, temperature and buffer conditions on the stability limit.
KeywordsHydroxyl Oligomer Fibril Turbidity Histidyl
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