Publication date: Available online 12 December 2013 Source:Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
Author(s): Daniel Huster
The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence each other; parameters such as acyl chain order, membrane thickness, membrane elasticity, permeability, lipid-domain and annulus formation are strongly modulated by proteins. More recent data also indicates that the influence of proteins goes beyond a single annulus of next-neighbor boundary lipids. Therefore, a mesoscopic approach to membrane lipid-protein interactions in terms of elastic membrane deformations has been developed. Solid-state NMR has greatly contributed to the understanding of lipid-protein interactions and the modern view of biological membranes. Methods that detect the influence of proteins on the membrane as well as direct lipid-protein interactions have been developed and are reviewed here. Examples for solid-state NMR studies on the interaction of Ras proteins, the antimicrobial peptide protegrin-1, the G protein-coupled receptor rhodopsin, and the K+ channel KcsA are discussed. This article is part of a Special Issue entitled Tools to study lipid functions.
[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.
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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.
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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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[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] Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Chem Phys Lipids. 2013 Sep 24;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation...
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Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Publication date: Available online 24 September 2013
Source:Chemistry and Physics of Lipids</br>
Author(s): Lei Zhang , Lishan Liu , Sergey Maltsev , Gary A. Lorigan , Carole Dabney-Smith</br>
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor...
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09-25-2013 11:15 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.
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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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[NMR paper] Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
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Biochim Biophys Acta. 2013 Apr 5;
Authors: Ciesielski F, Griffin DC, Rittig M, Moriyón I, Bonev BB
Abstract
Lipopolysaccharide (LPS) is a major component of the external leaflet of bacterial outer membranes, key pro-inflammatory factor and an important mediator of host-pathogen interactions. In host cells it activates the complement...
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[NMR paper] Solid-state NMR approaches to study protein structure and protein-lipid interactions.
Solid-state NMR approaches to study protein structure and protein-lipid interactions.
Solid-state NMR approaches to study protein structure and protein-lipid interactions.
Methods Mol Biol. 2013;974:357-87
Authors: Aisenbrey C, Michalek M, Salnikov ES, Bechinger B
Abstract
Solid-state NMR spectroscopy has been developed for the investigation of membrane-associated polypeptides and remains one of the few techniques to reveal high-resolution structural information in liquid-disordered phospholipid bilayers. In particular, oriented samples...
Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions
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