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Título

The diamagnetic susceptibility of the tubulin dimer

Autor Bras, W.; Torbet, J.; Diakun, Gregory P.; Rikken, G.L.J.A.; Díaz, José Fernando
Fecha de publicación 18-feb-2014
EditorHindawi Publishing Corporation
Citación Journal of Biophysics (2014) Article ID 985082, 5 pages
ResumenAn approximate value of the diamagnetic anisotropy of the tubulin dimer, Δχdimer, has been determined assuming axial symmetry and that only the α-helices and β-sheets contribute to the anisotropy. Two approaches have been utilized: (a) using the value for the Δχα for an α-helical peptide bond given by Pauling (1979) and (b) using the previously determined anisotropy of fibrinogen as a calibration standard. The Δχdimer≈4×10-27 JT-2 obtained from these measurements are similar to within 20%. Although Cotton-Mouton measurements alone cannot be used to estimate Δχ directly, the value we measured, CMdimer=1.41±0.03×10-8 T-2cm2mg-1, is consistent with the above estimate for Δχdimer. The method utilized for the determination of the tubulin dimer diamagnetic susceptibility is applicable to other proteins and macromolecular assemblies as well. © 2014 Wim Bras et al.
Descripción 6 p.-1 fig.
Versión del editorhttp://dx.doi.org/10.1155/2014/985082
URI http://hdl.handle.net/10261/99354
DOI10.1155/2014/985082
ISSN1687-8000
E-ISSN1687-8019
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