Schmid, Markus B. and Fleischmann, Matthias and D'Elia, Valerio and Reiser, Oliver and Gronwald, Wolfram and Gschwind, Ruth M. (2009) 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. CHEMBIOCHEM, 10 (3). 440-+. ISSN 1439-4227, 1439-7633
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | AMINOCYCLOPROPANE CARBOXYLIC-ACIDS; NMR-SPECTROSCOPY; RELATIVE CONFIGURATION; ALPHA/BETA-PEPTIDES; ALIGNMENT MEDIA; LINEAR PEPTIDES; ENHANCED NMR; RDCS; CRYSTALLOGRAPHY; PREDICTION; conformation analysis; NMR spectroscopy; peptides; peptidic foldamers; residual dipolar couplings; unnatural amino acids |
| Subjects: | 600 Technology > 610 Medical sciences Medicine 600 Technology > 660 Chemical engineering |
| Divisions: | Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner) Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 05 Oct 2020 09:59 |
| Last Modified: | 05 Oct 2020 09:59 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29473 |
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