Effect of the ordered interfacial water layer in protein complex formation: A nonlocal electrostatic approach.
Using a nonlocal electrostatic approach that incorporates the short-range structure of the contacting media, we evaluated the electrostatic contribution to the energy of the complex formation of two model proteins. In this study, we have demonstrated that the existence of an ordered interfacial water layer at the protein-solvent interface reduces the charging energy of the proteins in the aqueous solvent, and consequently increases the electrostatic contribution to the protein binding (change in free energy upon the complex formation of two proteins). This is in contrast with the finding of the continuum electrostatic model, which suggests that electrostatic interactions are not strong enough to compensate for the unfavorable desolvation effects.
Rubinstein
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Department of Biomedical Sciences and Surgery, Creighton University Medical Center, Omaha, Nebraska 68131, USA. arubinstein@mail.unomaha.edu
Sabirianov
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RF
Mei
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WN
Namavar
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F
Khoynezhad
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D003198:Computer Simulation; D004735:Energy Transfer; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D055672:Static Electricity; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D046912:Multiprotein Complexes; D011506:Proteins; D014867:Water