title: The structure and properties of horse muscle acylphosphatase in solution. Mobility of antigenic and active site regions.
abstract: The solution structure of acylphosphatase determined by proton nuclear magnetic resonance spectroscopy is described. The results allow us to discuss the fold of the protein (101 amino acids), to correlate the exposure and the mobility of the backbone with the antigenicity, and to locate the active site.
authors: Inorganic Chemistry Laboratory, University of Oxford, England.
authors: V
authors: V
authors: Saudek
authors: R J
authors: RJ
authors: Williams
authors: G
authors: G
authors: Ramponi
mesh_terms: D017766:Acid Anhydride Hydrolases; D000818:Animals; D001665:Binding Sites; D003198:Computer Simulation; D000939:Epitopes; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009038:Motion; D009132:Muscles / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000276:immunology; D011487:Protein Conformation; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000939:Epitopes; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase