title: Crystallographic studies of the dynamic properties of lysozyme.
abstract: The patterns of atomic displacements in the crystals of hen and human lysozyme derived from independent crystallographic refinement are broadly similar. Analysis of the pattern indicates a close correlation with molecular structure, strongly suggestive of intramolecular motion. The active site of lysozyme is located in a region of high displacement. It is concluded that protein mobility may play a significant part in biological activity and that X-ray crystallography can contribute to its analysis.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002645:Chickens; D005260:Female; D006801:Humans; D009038:Motion; D009113:Muramidase; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D009113:Muramidase