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NMR characterization of residual structure in the denatured state of protein L

论文类型 基础研究 发表日期 2014-10-14
来源 Journal of Molecular Biology
作者 Yi,Q.Alm,EJ.Baker,D.Scalley-Ki
关键词 Protein l Denatured state Residual structure Paramagnetic relaxation enhancement Nmr Chemical-shifts Folded proteins Binding domain Urea Prediction
摘要 Triple-resonance NMR experiments were used to assign the C-13(alpha), C-13(beta) N-15 and NH resonances for all the residues in the denatured state of a destabilized protein L variant in 2 M guanidine. The chemical shifts of most resonances were veryclose

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