Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures

Biochemistry. 1981 Aug 4;20(16):4667-76. doi: 10.1021/bi00519a023.


A densimetric investigation of the interactions between solvent components in glycerol-water mixtures (between 10 and 40 vol % glycerol) and seven proteins have been carried out in the acid pH region. All the proteins were found to be preferentially hydrated at all conditions used, i.e., addition of the proteins to the mixed solvent results in an increase in the chemical potential of glycerol. It is considered that this thermodynamically unfavorable interaction should tend to minimize the surface of contact between proteins and glycerol and in this way stabilize the native structure of globular proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Densitometry / methods
  • Drug Stability
  • Glycerol*
  • Hydrogen-Ion Concentration
  • Mathematics
  • Protein Conformation
  • Proteins*
  • Solvents
  • Thermodynamics
  • Water*


  • Proteins
  • Solvents
  • Water
  • Glycerol