Proceedings of the Royal Society of London A Mathematical and Physical Sciences · 1975 · 55 citations · 0 references
Life SciencesBiochemistryBiophysicsComputational ChemistryProtein BiochemistryStructural BiologyProtein CharacterizationProtein ChemistryProtein ConformationProtein StructureSolution-state Magnetic ResonanceSpectroscopy Of BiomoleculesElectron-nuclear Double ResonanceMagnetic Resonance Spectroscopy Of BiomoleculesNuclear ResonancesParamagnetic CentersParamagnetic SpeciesProtein Structure DeterminationSolvent EffectsSolvent Exchange
Abstract It is shown that many of the 1H resonances of a small protein, lysozyme, can be resolved by using very high magnetic fields and computational methods. The complete identification, or assignment, of the resolved resonances is closely linked to knowledge about the structure of the protein in solution. A brief and critical review is presented of assignment methods, including double resonance, multiplet structure measurements, pH titrations, site specific paramagnetic probes, intrinsic paramagnetic centres, solvent exchange, chemical modifications, and the specific binding properties of the protein. It is shown how these methods can be used to assign (a) to a particular class of 1H, e.g. NH or CH, (b) to a particular amino acid type and (c) to a particular amino acid in the protein.