The structure of cyclolinopeptide A in chloroform refined by RDC measurements | Zendy

Huben Krzysztof | Zendy; Jewgiński Michał | Zendy; Pabis Anna | Zendy; Paluch Piotr | Zendy; Luy Burkhard | Zendy; Jankowski Stefan | Zendy

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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.

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