On the Origin of NMR Dipolar Waves in Transient Helical Elements of Partially Folded Proteins

摘要

Residual dipolar couplings (RDCs) are powerful reporters of local conformational sampling in intrinsically unfolded or chemically denatured proteins, offering a powerful tool for studying molecular recognition and protein folding. Although RDCs have been used to identify transient helical formation within partially folded proteins, quantitative conformational interpretation has remained elusive. Experimental ~1D_(NH) RDCs previously measured in the S-peptide of ribonuclease A and N_(TAIL) (443-524), the C-terminal domain of the Sendai virus nucleoprotein, are shown in Figure 1.