Structural features of fab fragments of rheumatoid factor IgM-RF in solution

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dc.contributor.authorVolkov, VVen_AU
dc.contributor.authorLapuk, VAen_AU
dc.contributor.authorShtykova, EVen_AU
dc.contributor.authorStepina, NDen_AU
dc.contributor.authorDembo, KAen_AU
dc.contributor.authorSokolova, AVen_AU
dc.contributor.authorAmarantov, SVen_AU
dc.contributor.authorTimofeev, VPen_AU
dc.contributor.authorZiganshin, RKen_AU
dc.contributor.authorVarlamova, EYen_AU
dc.date.accessioned2009-06-09T06:06:34Zen_AU
dc.date.accessioned2010-04-30T05:06:52Zen_AU
dc.date.available2009-06-09T06:06:34Zen_AU
dc.date.available2010-04-30T05:06:52Zen_AU
dc.date.issued2008-05en_AU
dc.date.statistics2008-05en_AU
dc.description.abstractThe 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.en_AU
dc.identifier.citationVolkov, V. V., Lapuk, V. A., Shtykova, E. V., Stepina, N. D., Dembo, K. A., Sokolova, A. V., Amarantov, S. V., Timofeev, V. O., Ziganshin, R. K., & Valamova, E. Y. (2008). Structural features of fab fragments of rheumatoid factor IgM-RF in solution. Crystallography Reports, 53(3), 466-473. doi:10.1134/S1063774508030140en_AU
dc.identifier.govdoc1439en_AU
dc.identifier.issn1063-7745en_AU
dc.identifier.issue3en_AU
dc.identifier.journaltitleCrystallography Reportsen_AU
dc.identifier.pagination466-473en_AU
dc.identifier.urihttp://dx.doi.org/10.1134/S1063774508030140en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1315en_AU
dc.identifier.volume53en_AU
dc.language.isoenen_AU
dc.publisherSpringeren_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectImmunoglobulinsen_AU
dc.subjectElectron spin resonanceen_AU
dc.subjectMass spectroscopyen_AU
dc.subjectPeptidesen_AU
dc.subjectRheumatic diseasesen_AU
dc.titleStructural features of fab fragments of rheumatoid factor IgM-RF in solutionen_AU
dc.typeJournal Articleen_AU
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