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[Lysozyme Stabilization under High Pressure: Differential Scanning Microcalorimetry].

A Y Yegorov1,2, S A Potekhin3

  • 1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.

Molekuliarnaia Biologiia
|March 8, 2018
PubMed
Summary

High pressure affects lysozyme heat denaturation differently based on pH, with no impact on transition cooperativity. Lysozyme denaturation showed unusual positive volume changes, unlike most globular proteins.

Keywords:
denaturation volume changedifferential scanning microcalorimetryhigh pressurelysozyme

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Area of Science:

  • Biophysical Chemistry
  • Protein Chemistry

Background:

  • Lysozyme is a key model protein for studying denaturation.
  • Understanding protein behavior under pressure is crucial for various applications.

Purpose of the Study:

  • To investigate the effect of high pressure on lysozyme heat denaturation.
  • To analyze thermodynamic parameters and volume changes during denaturation.

Main Methods:

  • High-pressure differential scanning microcalorimetry was employed.
  • Experimental data were analyzed using a two-state equilibrium model.

Main Results:

  • Pressure influenced denaturation temperature and enthalpy variably with pH.
  • Transition cooperativity remained unaffected by pressure increases.
  • Lysozyme denaturation exhibited positive volume changes, an atypical observation.

Conclusions:

  • Pressure's effect on lysozyme denaturation is pH-dependent.
  • The observed positive volume change during lysozyme denaturation warrants further investigation into its underlying mechanisms.