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Correction: Trehalose-cored amphiphiles for membrane protein stabilization: importance of the detergent micelle size in GPCR stability
Manabendra
Das
a,
Yang
Du
b,
Jonas S.
Mortensen
c,
Manuel
Ramos
d,
Lubna
Ghani
a,
Ho Jin
Lee
a,
Hyoung Eun
Bae
a,
Bernadette
Byrne
e,
Lan
Guan
d,
Claus J.
Loland
c,
Brian K.
Kobilka
b and
Pil
Seok Chae
*a
aDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea. E-mail: pchae@hanyang.ac.kr
bMolecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA. E-mail: kobilka@stanford.edu
cDepartment of Neuroscience, University of Copenhagen, DK-2200, Copenhagen, Denmark. E-mail: cllo@sund.ku.dk
dDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA. E-mail: lan.guan@ttuhsc.edu
eDepartment of Life Sciences, Imperial College London, London, SW7 2AZ UK. E-mail: b.byrne@imperial.ac.uk
First published on 7th May 2019
Abstract
Correction for ‘Trehalose-cored amphiphiles for membrane protein stabilization: importance of the detergent micelle size in GPCR stability’ by Manabendra Das et al., Org. Biomol. Chem., 2019, 17, 3249–3257.
The authors regret that there were errors in the chemical structures of the amphiphiles in Fig. 2a and 3a. All the sugar units of TCG-C5 to TCM-C10 are identical (i.e. β-D-glucose for TCG-C5 to TCG-C7 and β-D-maltose for TCM-C8 to TCM-C10). The correct figures are shown below.
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| Fig. 1 (a) Synthetic scheme and chemical structures of newly prepared trehalose-cored amphiphiles (TCGs/TCMs/TCG-Ls). Novel amphiphiles were derived from α,α-trehalose via dibenzylidenated trehalose (A) and tetra-alkylated tetra-ol intermediates (B). The tetra-alkylated tetra-ol intermediates and TCGs/TCMs/TCG-Ls contain a C2 axis passing through the central part of the molecules, indicated by the blue dotted line on the chemical structures of the tetra-ol intermediate. The inset within circle (black) illustrates a known mechanism of β-selective glycosylation involving neighboring group participation (NGP). (b) Schematic representation of a membrane protein interacting with one of the new detergents following extraction from the membrane. | ||
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| Fig. 2 (a) The chemical structure of TCG-C5 is given to illustrate the axial anomeric protons (Ha and Ha′) and equatorial anomeric protons (He) and their couplings with the neighboring protons (H in blue color). (b) Partial 1H NMR spectrum in the anomeric region for TCG-C5 showing its high anomeric purity. The NMR spectrum of TCG-C5 gave two doublets at 4.64 and 4.34 ppm, along with a coupling constant (3Jaa) of 8.0 Hz, typical peak characteristics of β-anomeric protons. TCG-C5 also contains α-anomeric proton (He), giving doublets at 5.18 ppm with a reduced coupling constant (3Jae = 4.0 Hz). (c) A partial 13C NMR spectrum of TCG-C5. Only anomeric carbon signals for TCG-C5 are assigned. | ||
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
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