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|Title: ||Structural features of Fab fragments of rheumatoid factor IgM-RF in solution.|
|Authors: ||Volkov, VV|
|Keywords: ||Small Angle Scattering|
Electron Spin Resonance
|Issue Date: ||May-2008|
|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|
|Appears in Collections:||Journal Articles|
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