Structure determination of membrane proteins in native cellular membranes is critical to precisely reveal their structures in physiological conditions. However, it remains challenging for solid-state nuclear magnetic resonance (ssNMR) due to the low sensitivity and high complexity of ssNMR spectra of cellular membranes. Here, we present the structure determination of aquaporin Z (AqpZ) by ssNMR in Escherichia coli inner membranes. To enhance the signal sensitivity of AqpZ, we optimized protein...
[NMR paper] Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.
Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.
Related Articles Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.
Biology (Basel). 2020 Nov 12;9(11):
Authors: Yeh V, Goode A, Bonev BB
Abstract
Biological membranes define the interface of life and its basic unit, the cell. Membrane proteins play key roles in membrane functions, yet their structure and mechanisms remain poorly understood. Breakthroughs in crystallography and electron...
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11-19-2020 06:30 AM
[NMR paper] Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Nat Methods. 2013 Sep 8;
Authors: Wang S, Munro RA, Shi L, Kawamura I, Okitsu T, Wada A, Kim SY, Jung KH, Brown LS, Ladizhansky V
Abstract
Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning...
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09-10-2013 08:44 PM
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
J Biomol NMR. 2010 Sep;48(1):1-11
Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H
The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
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12-18-2010 12:00 PM
[NMR paper] Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Related Articles Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
J Am Chem Soc. 2005 Sep 21;127(37):12965-74
Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments...
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12-01-2010 06:56 PM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
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12-01-2010 06:56 PM
[NMR paper] Membrane protein structure determination using solid-state NMR.
Membrane protein structure determination using solid-state NMR.
Related Articles Membrane protein structure determination using solid-state NMR.
Methods Mol Biol. 2004;278:403-73
Authors: Watts A, Straus SK, Grage SL, Kamihira M, Lam YH, Zhao X
Solid-state NMR is emerging as a method for resolving structural information for large biomolecular complexes, such as membrane-embedded proteins. In principle, there is no molecular weight limit to the use of the approach, although the complexity and volume of data is still outside complete assignment...
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11-24-2010 09:25 PM
[NMR paper] Membrane protein structure determination by solid state NMR.
Membrane protein structure determination by solid state NMR.
Related Articles Membrane protein structure determination by solid state NMR.
Nat Prod Rep. 1999 Aug;16(4):419-23
Authors: Watts A, Burnett IJ, Glaubitz C, Gröbner G, Middleton DA, Spooner PJ, Watts JA, Williamson PT
Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane
Linear Mode
