Faculty Opinions recommendation of Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.

2011 ◽  
Author(s):  
Gottfried Otting
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Solid State Nmr ◽  
Isotope Labeling ◽  
Nmr Studies ◽  
Helical Protein ◽  
Uniform Isotope Labeling ◽  
Lipid Environment

One- and two-dimensional high-resolution solid-state NMR studies of zeolite lattice structures

1991 ◽  
Vol 91 (7) ◽  
pp. 1525-1543 ◽  
Author(s):  
C. A. Fyfe ◽  
Y. Feng ◽  
H. Grondey ◽  
G. T. Kokotailo ◽  
H. Gies
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Solid State Nmr ◽  
Lattice Structures ◽  
Two Dimensional ◽  
Nmr Studies ◽  
Zeolite Lattice

13C High resolution solid state NMR studies on cellulose samples of different physical structure

1983 ◽  
Vol 10 (1-2) ◽  
pp. 56-62 ◽  
Author(s):  
Jürgen Kunze ◽  
Gerhard Scheler ◽  
Bernd Schröter ◽  
Burkart Philipp
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Solid State Nmr ◽  
Physical Structure ◽  
Nmr Studies

ChemInform Abstract: One- and Two-Dimensional High-Resolution Solid-State NMR Studies of Zeolite Lattice Structures

ChemInform ◽  
2010 ◽  
Vol 23 (5) ◽  
pp. no-no
Author(s):  
C. A. FYFE ◽  
Y. FENG ◽  
H. GRONDEY ◽  
G. T. KOKOTAILO ◽  
H. GIES
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Solid State Nmr ◽  
Lattice Structures ◽  
Two Dimensional ◽  
Nmr Studies ◽  
Zeolite Lattice

Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies

2003 ◽  
Vol 30 (2) ◽  
pp. 253-261 ◽  
Author(s):  
Bethany Buck ◽  
Jamillah Zamoon ◽  
Tara L Kirby ◽  
Tara M DeSilva ◽  
Christine Karim ◽  
...  
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Solid State Nmr ◽  
Purification And Characterization ◽  
Nmr Studies

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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