[NMR paper] Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.
Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.
Related ArticlesShortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.
J Magn Reson. 2013 Nov 1;237C:175-181
Authors: Yamamoto K, Caporini MA, Im S, Waskell L, Ramamoorthy A
Abstract
Inherent low sensitivity of NMR spectroscopy has been a major disadvantage, especially to study biomolecules like membrane proteins. Recent studies have successfully demonstrated the advantages of performing solid-state NMR experiments at very low and ultralow temperatures to enhance the sensitivity. However, the long spin-lattice relaxation time, T1, at very low temperatures is a major limitation. To overcome this difficulty, we demonstrate the use of a copper-chelated lipid for magic angle spinning solid-state NMR measurements on cytochrome-b5 reconstituted in multilamellar vesicles. Our results on multilamellar vesicles containing as small as 0.5mol% of a copper-chelated lipid can significantly shorten T1 of protons, which can be used to considerably reduce the data collection time or to enhance the signal-to-noise ratio. We also monitored the effect of slow cooling on the resolution and sensitivity of (13)C and (15)N signals from the protein and (13)C signals from lipids.
PMID: 24246881 [PubMed - as supplied by publisher]
[NMR paper] Shortening Spin-lattice Relaxation Using a Copper-Chelated lipid at Low-Temperatures – A Magic Angle Spinning Solid-State NMR Study on a Membrane-Bound Protein
Shortening Spin-lattice Relaxation Using a Copper-Chelated lipid at Low-Temperatures – A Magic Angle Spinning Solid-State NMR Study on a Membrane-Bound Protein
Publication date: Available online 1 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Kazutoshi Yamamoto , Marc Caporini , Sangchoul Im , Lucy Waskell , Ayyalusamy Ramamoorthy</br>
Inherent low sensitivity of NMR spectroscopy has been a major disadvantage, especially to study biomolecules like membrane proteins. Recent studies have successfully demonstrated the advantages of performing...
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11-01-2013 03:48 AM
[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Nat Protoc. 2013 Nov;8(11):2256-70
Authors: Das N, Murray DT, Cross TA
Abstract
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[NMR paper] Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
Related Articles Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.
J Chem Phys. 2013 May 14;138(18):184201
Authors: Gopinath T, Veglia G
Abstract
We propose a general method that enables the acquisition of multiple 2D and 3D solid-state NMR spectra for U-(13)C, (15)N-labeled proteins. This method, called MEIOSIS (Multiple ExperIments via Orphan SpIn operatorS), makes...
Solid-state magic-angle spinning NMR of membrane proteins and protein–ligand interactions
Solid-state magic-angle spinning NMR of membrane proteins and protein–ligand interactions
April 2012
Publication year: 2012
Source:European Journal of Cell Biology, Volume 91, Issue 4</br>
</br>
Structural biology is developing into a universal tool for visualizing biological processes in space and time at atomic resolution. The field has been built by established methodology like X-ray crystallography, electron microscopy and solution NMR and is now incorporating new techniques, such as small-angle X-ray scattering, electron tomography, magic-angle-spinning solid-state...
[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] Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Related Articles Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Chembiochem. 2005 Sep;6(9):1679-84
Authors: Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H
Uniformly 13C-,15N-labelled outer-membrane protein G (OmpG) from Escherichia coli was expressed for structural studies by solid-state magic-angle spinning (MAS) NMR. Inclusion bodies of the recombinant, labelled protein...
Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.
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