Proton nuclear magnetic resonance study of bovine cytochrome oxidase

High-resolution proton nuclear magnetic resonance spectroscopy of cytochrome.

In cytochrome c the axial positions of the heme iron are occupied by two amino acid residues, one of which is known from X-ray studies to be histidyl. Nuclear magnetic resonance spectroscopy provides strong evidence that the sixth ligand is a methionyl residue in both the ferric and ferrous oxidation states. It is further shown that in cyanoferricytochrome c cyanide ion replaces methionyl in th...

NUCLEAR MAGNETIC RESONANCE STUDY OF THE STRUCTURE OF GLYOXALDIHYDRAZONE

Study of the nuclear magnetic resonance spectra of glyoxaldihydrazone in dimethylsulfoxide and deuterochlorofonn leads to the conclusion that this compound exists predominantly in non-chelate structure

Proton Nuclear Magnetic Resonance Spectroscopy

A proton nuclear magnetic resonance study of the conformation of bovine anaphylatoxin C5a in solution.

The solution conformation of bovine anaphylatoxin C5a has been investigated by nuclear magnetic resonance (NMR) spectroscopy. The 1H-NMR spectrum is assigned in a sequential manner using a variety of two-dimensional NMR techniques. A qualitative interpretation of the short range nuclear Overhauser enhancement data involving the NH, C alpha H and C beta H protons suggests that C5a has four helic...

Proton Nuclear Magnetic Resonance Study of Water in Flocs

Polymer/surfactant adsorption can lead to colloidal stability or particle flocculation, both of which are of importance in many industrial processes. Floc structure is one of the most important features of particle flocculation and this involves flOC-size, density and strength.1~ Spectroscopic techniques to investigate floc structure have been mainly limited to small-angle neutron scattering (S...