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Image Search Results
Journal: The Journal of Biological Chemistry
Article Title: The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence
doi: 10.1016/j.jbc.2022.101913
Figure Lengend Snippet: Dimerization of FlSp NT analyzed by SEC-MALS. Proteins purified at pH 5.5 and pH 8.0 were analyzed using a Superdex 75 increase SEC column equilibrated at each pH. The chromatograms show the differential refractive index (dRI, broken lines ) and light scattering signal (LS, solid lines ) at pH 5.5 ( red ) and pH 8.0 ( blue ) together with the molecular mass calculated by MALS at pH 5.5 ( orange ) and pH 8.0 ( cyan ). Representative measurements are shown for ( A ) WT FlSp NT, ( B ) FlSp NT∗, ( C ) FlSp NT E79QE84QE119Q , and ( D ) FlSp NT E79QE84QE119QE130Q . MALS data for FlSp NT E79QE84QE119QE130Q were associated with higher uncertainty (%). E , the experimentally determined average molecular masses were used to calculate the molecular weight ratio between pH 5.5 and pH 8.0 for each protein. FlSp, flagelliform spidroin; MALS, multiangle light scattering; NT, N-terminal; SEC, size-exclusion chromatography.
Article Snippet: The column was connected to a
Techniques: Purification, Refractive Index, Molecular Weight, Multi-Angle Light Scattering, Size-exclusion Chromatography