Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins

摘要

Over the last decade the accepted paradigm underpinning classical structural biology has been reassessed, with the general realization that a significant fraction of proteins encoded in eukaryotic genomes do not adopt a stable fold in their functional form, but instead are intrinsically disordered either in long contiguous regions, or in many cases throughout their entire length. The high degree of flexibility inherent to intrinsically disordered proteins (IDPs) bestows distinct properties allowing them to function differently to folded proteins, but this same attribute complicates characterization of their molecular behavior. To better understand the relationship between primary sequence and biological function in IDPs it is essential that calibrated techniques become available allowing a quantitative determination of their conformational behavior.