Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states.

Lignende værker

• Hydration of apomyoglobin in native, molten globule, and unfolded states by using microwave dielectric spectroscopy.
  af: Kamei, Takashi, et al.
  Udgivet: (2002)
• Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.
  af: Kobashigawa, Y., et al.
  Udgivet: (1999)
• The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry.
  af: Jamin, M., et al.
  Udgivet: (2000)
• Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy.
  af: Kreimer, D I, et al.
  Udgivet: (1994)
• Pressure-induced unfolding of the molten globule of all-Ala α-lactalbumin
  af: Lassalle, Michael W., et al.
  Udgivet: (2003)