Exchange of individual hydrogens for a protein in a crystal and in solution.
A preliminary comparison of the solvent exchange of individual hydrogens of a protein in solution and in a crystal has been possible by using data for lysozyme from 1H nuclear magnetic resonance and neutron diffraction studies. It is suggested that this approach enables a direct comparison of local dynamical behaviour in the two states. The results indicate markedly similar behaviour for many residues, but significant differences are indicated in several regions of the protein.
D000818:Animals; D002642:Chick Embryo; D003460:Crystallization; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase; D012542:Scattering, Radiation; D012996:Solutions; D014364:Tryptophan
D012996:Solutions; D006859:Hydrogen; D014364:Tryptophan; D009113:Muramidase