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Title: [IR-spectroscopic study of cytochrome C-phospholipid lipoprotein and proteolipid model membranes]. Author: Moshkov DA, Severina EP, Lazarev IuA, Boroviagin VL. Journal: Biofizika; 1975; 20(2):233-7. PubMed ID: 167868. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]