While solid-state NMR/DNP has become a well-established technique to significantly increase the signals of molecules embedded in homogeneous glassy matrices, the enhancement factors observed in heterogeneous and/or matrix-free samples lag somewhat behind. The possible reasons for such differences, present limitations, and future prospects of solid-state NMR/DNP are discussed in the context of membrane protein investigations. Membrane polypeptides and lipids are studied by MAS as well as oriented sample solid-state NMR approaches. Notably, even the more modest DNP signal enhancements obtained in such samples augment the signal intensities by 1–2 orders of magnitude, thus opening up new territory in structural biology by allowing the detection of new conformers, so far invisible intermediate states, or the acquisition of smaller quantities of membrane-associated polypeptides in much less time. New sample preparation protocols, dedicated instrumental hardware, and specifically designed biradicals have much improved the application of DNP to membranes using MAS and/or oriented solid-state NMR technologies.
[NMR paper] Alamethicin Supramolecular Organization in Lipid Membranes from (19)F Solid-State NMR.
Alamethicin Supramolecular Organization in Lipid Membranes from (19)F Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Alamethicin Supramolecular Organization in Lipid Membranes from (19)F Solid-State NMR.
Biophys J. 2016 Dec 06;111(11):2450-2459
Authors: Salnikov ES, Raya J, De Zotti M, Zaitseva E, Peggion C, Ballano G, Toniolo C, Raap J, Bechinger B
Abstract
Alamethicins (ALMs) are antimicrobial peptides of fungal...
[NMR paper] In-Cell Solid-State NMR: An Emerging Technique for the Study of Biological Membranes.
In-Cell Solid-State NMR: An Emerging Technique for the Study of Biological Membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles In-Cell Solid-State NMR: An Emerging Technique for the Study of Biological Membranes.
Biophys J. 2015 Dec 15;109(12):2461-6
Authors: Warnet XL, Arnold AA, Marcotte I, Warschawski DE
Abstract
Biological molecular processes are often studied in model systems, which simplifies their inherent complexity but may...
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Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes
Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes
Publication date: 21 April 2015
Source:Biophysical Journal, Volume 108, Issue 8</br>
Author(s): Xi Cheng , Sunhwan Jo , Yifei Qi , Francesca*M. Marassi , Wonpil Im</br>
Solid-state NMR has been used to determine the structures of membrane proteins in native-like lipid bilayer environments. Most structure calculations based on solid-state NMR observables are performed using simulated annealing with restrained molecular dynamics and an energy function, where all nonbonded...
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04-22-2015 03:33 PM
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
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Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Eur Biophys J. 2011 Jan 28;
Authors: Grasnick D, Sternberg U, Strandberg E, Wadhwani P, Ulrich AS
To better understand peptide-induced membrane fusion at a molecular level, we set out to determine the structure of the fusogenic peptide FP23 from the HIV-1 protein gp41 when bound to a lipid bilayer. An established solid-state...
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01-29-2011 12:35 PM
[NMR paper] Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd
Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd NMR.
Related Articles Exploring the calcium-binding site in photosystem II membranes by solid-state (113)Cd NMR.
Biochemistry. 2000 Jun 13;39(23):6751-5
Authors: Matysik J, Alia A, Nachtegaal G, van Gorkom HJ, Hoff AJ, de Groot HJ
Calcium (Ca(2+)) is an essential cofactor for photosynthetic oxygen evolution. Although the involvement of Ca(2+) at the oxidizing side of photosystem II of plants has been known for a long time, its ligand interactions and mode of...
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[NMR paper] Interaction of a type II myosin with biological membranes studied by 2H solid state N
Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
Related Articles Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
Biochemistry. 1998 Apr 21;37(16):5582-8
Authors: Arêas JA, Gröbner G, Glaubitz C, Watts A
Deuterium nuclear magnetic resonance spectroscopy (2H NMR) has been employed to investigate the interaction of lung type II myosin protein with neutral bilayers containing dimyristoylphosphatidylcholine (DMPC) as the only constituent and mixed bilayers containing...