title: Residual dipolar couplings in short peptidic foldamers: combined analyses of backbone and side-chain conformations and evaluation of structure coordinates of rigid unnatural amino acids.
abstract: A flexible tool for rigid systems. Residual dipolar couplings (RDCs) have proven to be valuable NMR structural parameters that provide insights into the backbone conformations of short linear peptidic foldamers, as illustrated here. This study demonstrates that RDCs at natural abundance can provide essential structural information even in the case of short linear peptides with unnatural amino acids. In addition, they allow for the detection of proline side-chain conformations and are used as a quality check for the parameterizations of rigid unnatural amino acids.
authors.affiliation: Institut für Organische Chemie, Universität Regensburg, Regensburg, Germany.
authors.forename: Markus B
authors.initials: MB
authors.lastname: Schmid
authors.forename: Matthias
authors.initials: M
authors.lastname: Fleischmann
authors.forename: Valerio
authors.initials: V
authors.lastname: D'Elia
authors.forename: Oliver
authors.initials: O
authors.lastname: Reiser
authors.forename: Wolfram
authors.initials: W
authors.lastname: Gronwald
authors.forename: Ruth M
authors.initials: RM
authors.lastname: Gschwind
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D008968:Molecular Conformation; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D000596:Amino Acids; D010455:Peptides