Conformational analysis of steroid hormone molecules in the lipid environment – A solid-state NMR approach

Steroids ◽  
2011 ◽  
Vol 76 (6) ◽  
pp. 558-563 ◽  
Author(s):  
Ping-Chen Shih ◽  
Guo-Chian Li ◽  
Kai-Jay Yang ◽  
Wenlung Chen ◽  
Der-Lii M. Tzou
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Solid State Nmr ◽  
Steroid Hormone ◽  
Lipid Environment

Solid-state NMR analysis of steroidal conformation of 17α- and 17β-estradiol in the absence and presence of lipid environment

Steroids ◽  
2012 ◽  
Vol 77 (3) ◽  
pp. 185-192 ◽  
Author(s):  
Guo-Chian Li ◽  
Da-Rong Wang ◽  
Wenlung Chen ◽  
Der-Lii M. Tzou
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Analysis ◽  
17Β Estradiol ◽  
Lipid Environment

scholarly journals Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs

Life ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 908
Author(s):  
Xing-Qi Dong ◽  
Jing-Yu Lin ◽  
Peng-Fei Wang ◽  
Yi Li ◽  
Jian Wang ◽  
...  
Keyword(s):  
Solid State ◽  
Chemical Shift ◽  
Solid State Nmr ◽  
Protein Structures ◽  
Anion Channel ◽  
Transmembrane Domains ◽  
Helical Structures ◽  
Nmr Studies ◽  
Two Samples ◽  
Lipid Environment

The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein into liposomes or retaining the protein in the native membrane of E. Coli., where it was expressed. The comparison of 13C-13C 2D correlation spectra between the two samples showed great similarity, opening the possibility to further study the acetate transport mechanism of SatP in its native membrane environment. Solid-state NMR studies also revealed small chemical shift differences of SatP in the two different membrane systems, indicating the importance of the lipid environment in determining the membrane protein structures and dynamics. Combining different 2D SSNMR spectra, chemical shift assignments were made on some sites, consistent with the helical structures in the transmembrane domains. In the end, we pointed out the limitation in the sensitivity for membrane proteins with such a size, and also indicated possible ways to overcome it.

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