title: Modulation of the intermolecular interaction of myoglobin by removal of the heme.
abstract: Toward understanding intermolecular interactions governing self-association of proteins, the present study investigated a model protein, myoglobin, using a small-angle X-ray scattering technique. It has been known that removal of the heme makes myoglobin aggregation-prone. The interparticle interferences of the holomyoglobin and the apomyoglobin were compared in terms of the structure factor. Analysis of the structure factor using a model potential of Derjaguin-Laudau-Verwey-Overbeek (DLVO) suggests that the intermolecular interaction potential of apomyoglobin is more attractive than that of holomyoglobin at short range from the protein molecule.
authors.affiliation: Graduate School of Advanced Integration Science, Chiba University, 1-33 Yayoi, Inage, Chiba 263-8522, Japan.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Imamura
authors.forename: Takeshi
authors.initials: T
authors.lastname: Morita
authors.forename: Tomonari
authors.initials: T
authors.lastname: Sumi
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Isogai
authors.forename: Minoru
authors.initials: M
authors.lastname: Kato
authors.forename: Keiko
authors.initials: K
authors.lastname: Nishikawa
mesh_terms: D006418:Heme / Q000302:isolation & purification*; D009211:Myoglobin / Q000737:chemistry* / Q000302:isolation & purification; D012542:Scattering, Radiation
chemical_list: D009211:Myoglobin; D006418:Heme
keywords: protein engineering; protein–protein interaction; small-angle X-ray scattering