Effect of calcium chloride on the conformation of proteins. Thermodynamic studies of some model compounds.
Partial molar heat capacities (CP2 degrees) and volumes (V2 degrees) for some amino acids and peptides were measured in 1 M aqueous calcium chloride solutions at 298.15 degrees K using a Picker flow microcalorimeter and an oscillating-tube digital density meter. Using the data for these amino acids and peptides in water, the corresponding partial molar heat capacities of transfer (CP2,tr degree) and volumes (V2,tr degree) from water to 1 M aqueous calcium chloride were deduced. These thermodynamic parameters are significantly positive, indicating that strong interactions occur between the ions of calcium chloride and the charged centres of these amino acids and peptides. A comparison has been made with a similar transfer of these compounds to sodium chloride solutions. The thermodynamic parameters of the transfer of peptide group (-CONH) are much more positive in calcium chloride than in sodium chloride solutions. The implication of this result for the ability of calcium chloride to act as a stronger destabilizer of protein conformation is discussed.
Bhat
R
R
Department of Chemistry, Indian Institute of Technology, New Delhi.
Ahluwalia
J C
JC
D000596:Amino Acids; D002122:Calcium Chloride / Q000494:pharmacology*; D002151:Calorimetry; D004151:Dipeptides; D011487:Protein Conformation / Q000187:drug effects*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D004151:Dipeptides; D002122:Calcium Chloride