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Dimerization analysis of wild-type and mutant END domains by SEC/SLS and NMR.

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https://figshare.com/articles/dataset/_Dimerization_analysis_of_wild_type_and_mutant_END_domains_by_SEC_SLS_and_NMR_/1430596
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ND—Not determined. Protein sample not stable and/or not suitable for NMR analysis. A Molecular weights were calculated from refractive index (RI) and right angle light scattering (RALS) data (Fig D in S1 Text). B For NMR, proteins without a Z-tag were analyzed. C 2D 1H,15N-HSQC spectrum indicates the presence of two populations, interpreted as an equilibrium between a folded dimer and the unfolded monomer of the END domain (Fig D in S1 Text). Dimerization analysis of wild-type and mutant END domains by SEC/SLS and NMR.
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2015-05-29
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