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.
KeywordsDynamic Light Scattering Critical Pressure Association Process Altered Precipitate Histidyl Residue
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M. Fändrich, M.A. Fletcher and C.M. Dobson (2002): Amyloid Fibrils From Muscle Myoglobin. Nature
, 165–166 (2001).CrossRefGoogle Scholar
B. Gorovits, P.M. Horowitz (1998): High Hydrostatic Pressure Can Reverse Aggregation of Protein Folding Intermediates and Facilitate Acquisition of Native Structure, Biochemistry
37, 6132–6135.CrossRefGoogle Scholar
A. Zipp, W. Kautzmann (1973): Pressure denaturation of metmyoglobin, Biochemistry
, 4217–4228.CrossRefGoogle Scholar
L. Smeller (2002): Pressure-temperature phase diagrams of biomolecules, Biochim. Biophys. Acta
, 11–29.CrossRefGoogle Scholar
L. Smeller, P. Rubens, K. Heremans (1999): Pressure Effect on the Temperature-Induced Unfolding and Tendency To Aggregate of Myoglobin, Biochemistry
, 3816–3820.CrossRefGoogle Scholar
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