Salt bridge interactions: stability of the ionic and neutral complexes in the gas phase, in solution, and in proteins.
A theoretical study on the stability of the salt bridges in the gas phase, in solution, and in the interior of proteins is presented. The study is mainly focused on the interaction between acetate and methylguanidinium ions, which were used as model compounds for the salt bridge between Asp (Glu) and Arg. Two different solvents (water and chloroform) were used to analyze the effect of varying the dielectric constant of the surrounding media on the salt bridge interaction. Calculations in protein environments were performed by using a set of selected protein crystal structures. In all cases attention was paid to the difference in stability between the ion pair and neutral hydrogen-bonded forms. Comparison of the results determined in the gas phase and in solution allows us to stress the large influence of the environment on the binding process, as well as on the relative stability between the ionic and neutral complexes. The high anisotropy of proteins and the local microenvironment in the interior of proteins make a decisive contribution in modulating the energetics of the salt bridge. In general, the formation of salt bridges in proteins is not particularly favored, with the ion pair structure being preferred over the interaction between neutral species.
Barril
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Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Spain.
Alemán
C
C
Orozco
M
M
Luque
F J
FJ
D000085:Acetates; D001120:Arginine / Q000737:chemistry*; D001224:Aspartic Acid / Q000737:chemistry*; D002725:Chloroform; D004735:Energy Transfer; D019791:Guanidine; D007477:Ions; D009716:Numerical Analysis, Computer-Assisted; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D014867:Water
D000085:Acetates; D007477:Ions; D011506:Proteins; D012996:Solutions; D014867:Water; D001224:Aspartic Acid; D002725:Chloroform; D001120:Arginine; D019791:Guanidine