[Study of Monomolecular layers of immunoglobulin G by IR-spectroscopy].
The deposited immunoglobulin G (IgG) monomolecular layers consisting of native protein molecules oriented either horizontally or vertically towards the Si internal reflection plate, and also of molecules, denatured in monolayers at air-water interface have been studied by attenuated total-reflection (ATR) IR-spectroscopy technique. It was shown that deposition of IgG molecules on Si surface from monolayers at air--water interface did not change conformation and orientation of the molecules. The value of monolayer thickness correlates with the IgG molecule dimensions calculated from X-ray diffraction data. It was also established that beta-conformation prevails in the secondary structure of both native and denaturated molecules.
D000818:Animals; D006736:Horses; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D011487:Protein Conformation; D011489:Protein Denaturation; D013055:Spectrophotometry, Infrared / Q000379:methods; D014961:X-Ray Diffraction
D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G
Issledovanie monomolekuliarnykh sloev immunoglobulina G metodom IK-spektroskopii.