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An approximate value of the diamagnetic anisotropy of the tubulin dimer, Δ χ   dimer , 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 Δ χ    α   for an   α  -helical peptide bond given by Pauling (1979) and (b) using the previously determined anisotropy of fibrinogen as a calibration standard. The Δ χ   dimer  ≈ 4 × 10 −27  JT −2  obtained from these measurements are similar to within 20%. Although Cotton-Mouton measurements alone cannot be used to estimate Δ χ  directly, the value we measured, CM dimer  = (1.41 ± 0.03) × 10 −8  T −2 cm 2 mg −1 , is consistent with the above estimate for Δ χ   dimer . The method utilized for the determination of the tubulin dimer diamagnetic susceptibility is applicable to other proteins and macromolecular assemblies as well.

The Diamagnetic Susceptibility of the Tubulin Dimer