ConspectusMembrane proteins mediate a plethora of cellular functions and represent important targets for drug development. Unlike soluble proteins, membrane proteins require native-like environments to fold correctly and be active. Therefore, modern structural biology techniques have aimed to determine the structure and dynamics of these membrane proteins at physiological temperature and in liquid crystalline lipid bilayers. With the flourishing of new NMR methodologies and improvements in...
[NMR paper] Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
Related Articles Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
J Phys Chem B. 2018 Feb 19;:
Authors: Banigan JR, Leninger M, Her AS, Traaseth NJ
Abstract
It is known that the lipid composition within a cellular membrane can influence membrane protein structure and function. In this Article, we...
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
From The DNP-NMR Blog:
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
This article is not about DNP. However, the authors describe how to use paramagnetic relaxation enhancers to speed up the data acquisition and with this increase the sensitivity. A similar effect happens when a paramagnetic polarization agent is used in a DNP-NMR experiment and often the only reason why it is actually possible to run 1H-DNP-NMR experiments with recycling delays of several seconds...
[NMR paper] Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Related Articles Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
J Biomol NMR. 2013 Dec 4;
Authors: Ullrich SJ, Hölper S, Glaubitz C
Abstract
A considerable limitation of NMR spectroscopy is its inherent low sensitivity. Approximately 90*% of the measuring time is used by the spin system to return to its Boltzmann equilibrium after excitation, which is...
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[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 Articles 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.
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...
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11-20-2013 12:52 PM
[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
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?
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