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| Title: | Structural features of Fab fragments of rheumatoid factor IgM-RF in solution. |
| Authors: | Volkov, VV Lapuk, VA Shtykova, EV Stepina, ND Dembo, KA Sokolova, AV Amarantov, SV Timofeev, VP Ziganshin, RK Varlamova, EY |
| Keywords: | Small Angle Scattering Immunoglobulins Electron Spin Resonance Mass Spectroscopy Peptides Rheumatic Diseases |
| Issue Date: | May-2008 |
| Publisher: | Springer |
| Citation: | Volkov, V. V., Lapuk, V. A., Shtykova, E. V., Stepina, N. D., Dembo, K. A., Sokolova, A. V., et al. (2008). Structural features of Fab fragments of rheumatoid factor IgM-RF in solution. Crystallography Reports, 53(3), 466-473. |
| Abstract: | The structural features of the Fab fragments of monoclonal (Waldenstrom's disease) immunoglobulin M (I-M) and rheumatoid immunoglobulin M (lgM-RF) were studied by a complex of methods, including small-angle X-ray scattering (SAXS), electron spin resonance (ESR), and mass spectrometry (MS). The Fab-RF fragment was demonstrated to be much more flexible in the region of interdomain contacts, the molecular weights and the shapes of the Fab and Fab-RF macromolecules in solution being only slightly different. According to the ESR data, the rotational correlation time for a spin label introduced into the peptide sequence for Fab is twice as large as that for Fab-RF (21 +/- 2 and 11 +/- 1 ns, respectively), whereas the molecular weights of these fragments differ by only 0.5% (mass-spectrometric data), which correlates with the results of molecular-shape modeling by small-angle X-ray scattering. The conclusion about the higher flexibility of the Fab-RF fragment contributes to an understanding of the specificity of interactions between the rheumatoid factor and the anti-ens of the own organism. © 2008, Springer. The original publication is available at www.springerlink.com |
| URI: | http://dx.doi.org/10.1134/S1063774508030140 http://apo.ansto.gov.au/dspace/handle/10238/1315 |
| ISSN: | 1063-7745 |
| Appears in Collections: | Journal Articles
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