title: Using chemical shifts to assess transient secondary structure and generate ensemble structures of intrinsically disordered proteins.
abstract: The chemical shifts of backbone atoms in polypeptides are sensitive to the dihedral angles phi and psi and can be used to estimate transient secondary structure and to generate structural ensembles of intrinsically disordered proteins (IDPs). In this chapter, several of the random coil reference databases used to estimate transient secondary structure are described, and the procedure is outlined for using these databases to estimate transient secondary structure. A new protocol is also presented for generating a diverse ensemble of structures for an IDP and reweighting these structures to optimize the fit between simulated and experimental chemical shift values.
authors: Department of Physics, University of Idaho, Moscow, ID, USA.
authors: Stepan
authors: S
authors: Kashtanov
authors: Wade
authors: W
authors: Borcherds
authors: Hongwei
authors: H
authors: Wu
authors: Gary W
authors: GW
authors: Daughdrill
authors: F Marty
authors: FM
authors: Ytreberg
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D030562:Databases, Protein; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D016159:Tumor Suppressor Protein p53