Backbone ¹H, ¹⁵N, and ¹³C and side chain ¹³Cβ NMR chemical shift assignment of murine interleukin-10
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Updated: May 8, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Georg Künze1, Stephan Theisgen, Daniel Huster
1Institute of Medical Physics and Biophysics, University of Leipzig, Härtelstraße 16/18, 04107, Leipzig, Germany, Georg.Kuenze@medizin.uni-leipzig.de.
Almost complete assignment of backbone (1)H, (13)C, (15)N and side chain (13)Cβ resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point mutation C149Y was introduced to suppress incorrect disulfide bond formation and to improve protein refolding.
Almost complete assignment of backbone (1)H, (13)C, (15)N and side chain (13)Cβ resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point mutation C149Y was introduced to suppress incorrect disulfide bond formation and to improve protein refolding.
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