Surface properties are highly sensitive to small ph induced changes in the 3-D structure of alpha-lactalbumin.

Míreanna comhchosúla

• Heat treatment of bovine alpha-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity.
  de réir: Wijesinha-Bettoni, R, et al.
  Foilsithe / Cruthaithe: (2007)
• Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules.
  de réir: Wijesinha-Bettoni, R, et al.
  Foilsithe / Cruthaithe: (2001)
• Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.
  de réir: Wijesinha-Bettoni, R, et al.
  Foilsithe / Cruthaithe: (2001)
• Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH.
  de réir: Smith, L, et al.
  Foilsithe / Cruthaithe: (1999)
• Partially folded forms of barley lipid transfer protein are more surface active.
  de réir: Clare Mills, E, et al.
  Foilsithe / Cruthaithe: (2009)