The structure of cyclolinopeptide A in chloroform refined by RDC measurements
| Autor: | Krzysztof Huben, Anna Pabis, Michał Jewgiński, Stefan Jankowski, Piotr Paluch, Burkhard Luy |
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| Rok vydání: | 2014 |
| Předmět: |
Pharmacology
Coupling constant Chloroform Organic Chemistry General Medicine Nuclear Overhauser effect Nuclear magnetic resonance spectroscopy Biochemistry Crystal chemistry.chemical_compound Nuclear magnetic resonance chemistry Structural Biology Residual dipolar coupling Drug Discovery Molecular Medicine Physical chemistry Molecule Molecular Biology Vicinal |
| Zdroj: | Journal of Peptide Science. 20:901-907 |
| ISSN: | 1075-2617 |
| DOI: | 10.1002/psc.2683 |
| Popis: | Three-dimensional structures of molecules traditionally assigned from nuclear Overhauser effects and vicinal coupling constants are recently complemented by measurements of residual dipolar couplings. Residual dipolar couplings measured in a stretched poly(dimethylsiloxane) gel were used to determine the structure of cyclolinopeptide A in chloroform solution at −50 °C. After structure refinement, conformational details of main cluster were discussed in relation to crystal and nuclear Overhauser effect derived structures. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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