[Comparison of the structures of different forms of sperm whale myoglobin in solution using wide angle x-ray scattering].

Experimental X-ray diffuse scattering curves in a wide range of angles for oxy-, deoxy-, met- and cyan-forms of sperm whale myoglobin in solution have been obtained. It has been found that scattering indicatrices of these ligand forms of myoglobin are well compatible with each other and differ from the theoretical scattering curve of met-myoglobin, calculated from the structure of this protein in crystal. The conclusions have been drawn: (1) on the similarity of myoglobin structures in solution for all the protein forms studied; (2) on the difference in the structure of the above ligand forms of myoglobin in solution from the structure of the protein in crystal by a slight shift (about 2 A) of the "hairpin" GH.