The enthalpy of interaction of urea with some globular proteins.
The enthalpies of interaction of urea with five globular proteins, ribonuclease A, trypsin, beta-lacto-globulin, ovalbumin and bovine serum albumin have been measured in aqueous solution at pH 7.0, I=0.005 M and 25 degrees C over a range of urea molality m from 0-15 mmol g-1 (where a 1 molal solution contains 1 mmol g-1). For all the proteins the interaction is exothermic, and there is an appreciable heat evolution at low urea concentrations, m less than 5 mmol g-1, which increases sharply at higher urea concentrations when the proteins undergo unfolding. If account is taken of the endothermic enthalpies of unfolding of the native proteins, the enthalpies of interactions of urea per unit mass denatured protein lie in the range -45 to -75 J g-1, corresponding to an average binding enthalpy of -23 kJ mol-1 bound urea.
D001665:Binding Sites; D007700:Kinetics; D007782:Lactoglobulins; D010047:Ovalbumin; D011485:Protein Binding; D011487:Protein Conformation; D012260:Ribonucleases; D012710:Serum Albumin, Bovine; D013816:Thermodynamics; D014357:Trypsin; D014508:Urea
D007782:Lactoglobulins; D012710:Serum Albumin, Bovine; D014508:Urea; D010047:Ovalbumin; D012260:Ribonucleases; D014357:Trypsin