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.
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.
Schmid
Markus B
MB
Institut für Organische Chemie, Universität Regensburg, Regensburg, Germany.
Fleischmann
Matthias
M
D'Elia
Valerio
V
Reiser
Oliver
O
Gronwald
Wolfram
W
Gschwind
Ruth M
RM
D000596:Amino Acids / Q000737:chemistry*; D008968:Molecular Conformation; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D000596:Amino Acids; D010455:Peptides