- 作者: Someswar Chatterjee and I. Basumallick*
- 作者服務機構: Department of Chemistry, Visva-Bharati, Santiniketan-731235, India
- 中文摘要: Free energies of transfer (ΔGt) of RibonucleaseA (RNaseA) from water to aqueous solutions of urea (4 M, 6 M and 8 M), a protein denaturing solvent as well as ΔGt of RibonucleaseA, β-Lactoglobulin, α-Chymotripsin and ChymotrypsinogenA from water to aqueous glycerol (10%, 20%, 30% and 40%), a protein stabilizing solvent has been dissected into cavity term [ΔGt(cav)] and interaction term [ΔGt(int)]. The interaction free energy includes all types of interactions like hard-soft, hydrogen bonding, electrostatic, etc. The cavity forming free energies have been calculated using the standard version of scaled particle theory (SPT) with well-reported SPT parameters. It has been found that transfer free energies of cavity terms ΔGt(cav) for native protein from water to urea-water and water to aqueous glycerol follow almost opposite trends. This primarily indicates there may be some correlation between cavity creation energies and protein denaturing and stabilizing ability of a solvent. The results are in agreement with those obtained from preferential binding coefficient studies in these media.
- 英文摘要: --
- 中文關鍵字: Cavity forming free energy; Denaturing solvent; Protein stabilization; RibonucleaseA; Scaled particle theory.
- 英文關鍵字: --