Si-Hyung Lee, Do-Hyoung Kim, Joan J. Han, Eun-Ji Cha, Ji-Eun Lim, Ye-Jin Cho, Chewook Lee and Kyou-Hoon Han Pages 34 - 54 ( 21 )
Intrinsically unfolded proteins (IUPs) do not obey the golden rule of structural biology, 3D structure = function, as they manifest their inherent functions without resorting to three-dimensional structures. Absence of a compact globular topology in these proteins strongly implies that their ligand recognition processes should involve factors other than spatially well-defined binding pockets. Heteronuclear multidimensional (HetMulD) NMR spectroscopy assisted with a stable isotope labeling technology is a powerful tool for quantitatively investigating detailed structural features in IUPs. In particular, it allows us to delineate the presence and locations of pre-structured motifs (PreSMos) on a per-residue basis. PreSMos are the transient local structural elements that presage target-bound conformations and act as specificity determinants for IUP recognition by target proteins. Here, we present a brief chronicle of HetMulD NMR studies on IUPs carried out over the past two decades along with a discussion on the functional significance of PreSMos in IUPs.
PreSMos (Pre-Structured Motifs), IUPs (Intrinsically Unfolded Proteins), NMR, IDR (Intrinsically Disordered Region), Mostly Unstructured (MU), Completely Unstructured (CU), IDPs, NUPs, Polypeptide, amphipathic helix
Biomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, 125 Gwahak-ro, Yuseong-gu, Daejeon, 305-806 Korea.