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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
Author(s) -
Schmid Markus B.,
Fleischmann Matthias,
D'Elia Valerio,
Reiser Oliver,
Gronwald Wolfram,
Gschwind Ruth M.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800736
Subject(s) - side chain , chemistry , amino acid , residual dipolar coupling , residual , dipole , stereochemistry , crystallography , computational chemistry , combinatorial chemistry , nuclear magnetic resonance spectroscopy , organic chemistry , biochemistry , algorithm , polymer , computer science
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.