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The structure of cyclolinopeptide A in chloroform refined by RDC measurements
Author(s) -
Huben Krzysztof,
Jewgiński Michał,
Pabis Anna,
Paluch Piotr,
Luy Burkhard,
Jankowski Stefan
Publication year - 2014
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2683
Subject(s) - vicinal , residual dipolar coupling , chloroform , chemistry , nuclear overhauser effect , crystal structure , dipole , molecule , residual , coupling constant , nuclear magnetic resonance spectroscopy , computational chemistry , crystallography , stereochemistry , organic chemistry , physics , algorithm , particle physics , computer science
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.