The influence of molecular variation on protein interactions.
We investigated the influence of solvation forces on protein-protein interactions for two forms of lysozyme: hen egg white (HEWL) and turkey egg white (TEWL). Turkey egg white has more surface exposed hydrophobic residues than HEWL and the protein-protein interactions of TEWL are shown to be more attractive than those of HEWL, for the conditions studied. The importance of including a solvation term in the potential of mean force model, to account for molecular variation in protein surface characteristics, is highlighted. We also show that the magnitude of this solvation term can be estimated using readily available data.
Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom.
Jason G S
JG
Ho
Anton P J
AP
Middelberg
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003198:Computer Simulation; D019281:Dimerization; D004527:Egg Proteins / Q000737:chemistry; D004735:Energy Transfer; D008956:Models, Chemical; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry* / Q000145:classification; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D012965:Sodium Chloride / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D013314:Stress, Mechanical; D014422:Turkeys; D014961:X-Ray Diffraction
D004527:Egg Proteins; D011506:Proteins; D012997:Solvents; D012965:Sodium Chloride; D009113:Muramidase