Ras acts as a molecular switch to control intracellular signaling on the plasma membrane (PM). Elucidating how Ras associates with PM in the native cellular environment is crucial for understanding its control mechanism. Here, we used in-cell nuclear magnetic resonance (NMR) spectroscopy combined with site-specific ^(19)F-labeling to explore the membrane-associated states of H-Ras in living cells. The site-specific incorporation of p-trifluoromethoxyphenylalanine (OCF(3)Phe) at three different...
[NMR paper] Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR
Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR
Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28...
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[NMR paper] Dynamics properties of membrane proteins in native cell membranes revealed by solid-state NMR spectroscopy
Dynamics properties of membrane proteins in native cell membranes revealed by solid-state NMR spectroscopy
Cell membranes provide an environment that is essential to the functions of membrane proteins. Cell membranes are mainly composed of proteins and highly diverse phospholipids. The influence of diverse lipid compositions of native cell membranes on the dynamics of the embedded membrane proteins has not been examined. Here we employ solid-state NMR to investigate the dynamics of E. coli Aquaporin Z (AqpZ) in its native inner cell membranes, and reveal the influence of diverse lipid...
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[NMR paper] Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Related Articles Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.
Nat Protoc. 2021 Jan 13;:
Authors: Narasimhan S, Pinto C, Lucini Paioni A, van der Zwan J, Folkers GE, Baldus M
Abstract
For a long time, solid-state nuclear magnetic resonance (ssNMR) has been employed to study complex biomolecular systems at the detailed chemical, structural, or dynamic level. Recent progress in...
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[ASAP] Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies
Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00423/20200724/images/medium/bi0c00423_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00423
http://feeds.feedburner.com/~r/acs/bichaw/~4/WFH3x3vJplk
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[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
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[NMR paper] Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy.
Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy.
Related Articles Direct observation of the ion-pair dynamics at a protein-DNA interface by NMR spectroscopy.
J Am Chem Soc. 2013 Feb 14;
Authors: Anderson KM, Esadze A, Manoharan M, Bruschweiler R, Gorenstein DG, Iwahara J
Abstract
Ion pairing is one of the most fundamental chemical interactions and is essential for molecular recognition by biological macromolecules. From an experimental standpoint, very little is known to date about ion-pair...
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[NMR paper] Direct observation of cell wall structure in living plant tissues by solid-state C NM
Direct observation of cell wall structure in living plant tissues by solid-state C NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Direct observation of cell wall structure in living plant tissues by solid-state C NMR spectroscopy.
Plant Physiol. 1990 Jan;92(1):61-5
Authors: Jarvis MC, Apperley DC
Solid-state (13)C nuclear magnetic resonance (NMR) spectra of the following intact plant tissues were recorded by the crosspolarization...