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Solution NMR Structure of Proteorhodopsin
Author(s) -
Reckel Sina,
Gottstein Daniel,
Stehle Jochen,
Löhr Frank,
Verhoefen MirkaKristin,
Takeda Mitsuhiro,
Silvers Robert,
Kainosho Masatsune,
Glaubitz Clemens,
Wachtveitl Josef,
Bernhard Frank,
Schwalbe Harald,
Güntert Peter,
Dötsch Volker
Publication year - 2011
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/anie.201105648
Subject(s) - library science , chemistry , art history , physics , philosophy , art , computer science
A solved puzzle : The structure of the seven‐transmembrane‐helix proton pump proteorhodopsin obtained by solution NMR spectroscopy is based on NOE data combined with distance restraints derived from paramagnetic relaxation enhancement (see picture). Restraints from residual dipolar couplings improved the structural accuracy.