Nov, 2013
Modulation of the intermolecular interaction of myoglobin by removal of the heme
JOURNAL OF SYNCHROTRON RADIATION
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- Volume
- 20
- Number
- First page
- 919
- Last page
- 922
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1107/S0909049513022772
- Publisher
- WILEY-BLACKWELL
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.
- Link information
- ID information
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- DOI : 10.1107/S0909049513022772
- ISSN : 0909-0495
- eISSN : 1600-5775
- Web of Science ID : WOS:000325639200022