Open AccessModulation of the intermolecular interaction of myoglobin by removal of the heme
Author(s) -
Imamura Hiroshi,
Morita Takeshi,
Sumi Tomonari,
Isogai Yasuhiro,
Kato Minoru,
Nishikawa Keiko
Publication year - 2013
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049513022772
Subject(s) - myoglobin , intermolecular force , heme , chemistry , dlvo theory , hemeprotein , intermolecular interaction , crystallography , biophysics , chemical physics , molecule , biochemistry , organic chemistry , biology , colloid , enzyme
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.