NMR characterization of residual structure in the denatured state of protein L
| 論文類型 | 基礎(chǔ)研究 | 發(fā)表日期 | 2014-10-14 |
| 來源 | Journal of Molecular Biology | ||
| 作者 | Yi,Q.Alm,EJ.Baker,D.Scalley-Ki | ||
| 關(guān)鍵詞 | 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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