[IR-spectroscopic study of cytochrome C-phospholipid lipoprotein and proteolipid model membranes].
It is shown by the methods of IR-spectroscopy and peptide hydrogen-deuterium exchange that a) considerable changes in the protein spectra occur (beta-conformation in the protein structure appears) during the interaction in water of cytochrome c molecules with lipid membranes containing negatively charged polar groups; b) further significant changes of the protein spectrum occur under the action of 1% OsO4 and heating up to n plus 95 degrees C; c) the conformational state of the pure protein in water; after the treatments of the proteolipid memebranes with 1% OsO4 and heating up to n degrees C no significant changes of protein spectrum occur, that may suggest hydrophobic interactions between the protein and lipids; d) the treatment of both pure cytichrome c and the model membranes with 1% glutaraldehyde, 30, 60% ethanol and acetone solutions in water does not reveal substantial changes in IR-spectra of the protein moiety.
D003574:Cytochrome c Group; D006358:Hot Temperature; D008074:Lipoproteins; D008567:Membranes, Artificial; D008968:Molecular Conformation; D009992:Osmium; D010743:Phospholipids; D011489:Protein Denaturation; D013055:Spectrophotometry, Infrared
D003574:Cytochrome c Group; D008074:Lipoproteins; D008567:Membranes, Artificial; D010743:Phospholipids; D009992:Osmium
Isseldovanie tsitokhrom-c-fosfolipidnykh lipoproteinovykh i proteolipidykh model'nykh membran metodom IK-spektroskopii