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De Novo Structure Determination from Residual Dipolar Couplings by NMR Spectroscopy
Author(s) -
Simon Bernd,
Sattler Michael
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020201)41:3<437::aid-anie437>3.0.co;2-3
Subject(s) - residual dipolar coupling , nuclear magnetic resonance spectroscopy , residual , fluorine 19 nmr , nuclear magnetic resonance , spectroscopy , chemistry , materials science , physics , computer science , algorithm , quantum mechanics
The three‐dimensional structures of biomacromolecules in solution can be determined with NMR spectroscopy. The use of residual dipolar couplings (RDCs) that can be measured in dilute liquid crystalline solution is currently revolutionizing the way structures are determined by NMR spectroscopy. This is highlighted by the recent de novo structure determination of the protein ubiquitin (see picture; liquid crystals are shown in green) using only RDC data.