Modulation of the intermolecular interaction of myoglobin by removal of the heme
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 interfer...
| Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 20(2013), Pt 6 vom: 07. Nov., Seite 919-22 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2013
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| Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't protein engineering protein–protein interaction small-angle X-ray scattering Myoglobin Heme 42VZT0U6YR |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 22.05.2014 Date Revised 18.05.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1600-5775 |
| DOI: | 10.1107/S0909049513022772 |