title: [Study of apocytochrome c from the horse heart by high resolution 1H NMR].
abstract: The horse heart apocytochrome c was investigated by high resolution 1H-NMR. The secondary chemical shifts of 1H-NMR spectra are not observed, which is typical for disordered molecules. However NOE is characterized by the appearance of spin diffusion which decreases with a temperature increase. The presence of spin diffusion assumes an existence of rigid sites and thus some ordered conformation of the molecule.
authors.forename: V P
authors.initials: VP
authors.lastname: Kutyshenko
mesh_terms: D000818:Animals; D001059:Apoproteins / Q000032:analysis*; D003574:Cytochrome c Group / Q000032:analysis*; D045304:Cytochromes c; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D009206:Myocardium / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D001059:Apoproteins; D003574:Cytochrome c Group; D045304:Cytochromes c
vernacular_title: Issledovanie apotsitokhroma c iz serdtsa loshadi metodom 1H IaMR vysokogo razresheniia.