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Pressure-induced Critical Association of Myoglobin

  • R. Gebhardt
  • W. Doster
  • J. Friedrich
  • W. Petry
  • A. Schulte
Conference paper

Abstract

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.

Keywords

Dynamic Light Scattering Critical Pressure Association Process Altered Precipitate Histidyl Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • R. Gebhardt
    • 1
  • W. Doster
    • 1
  • J. Friedrich
    • 2
  • W. Petry
    • 1
  • A. Schulte
    • 1
  1. 1.Physics Department E13Technical University MunichGarchingGermany
  2. 2.Physics Department E14Technical University MunichGarchingGermany

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