Studying Lateral Diffusion in Lipid Bilayers by Combining a Magic Angle Spinning NMR Probe with a Microimaging Gradient System

2004 ◽  
Vol 126 (31) ◽  
pp. 9534-9535 ◽  
Author(s):  
André Pampel ◽  
Klaus Zick ◽  
Hartmut Glauner ◽  
Frank Engelke
Keyword(s):  
Lipid Bilayers ◽  
Lateral Diffusion ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Gradient System ◽  
Angle Spinning

scholarly journals Virus Structures and Dynamics by Magic-Angle Spinning NMR

2021 ◽  
Vol 8 (1) ◽  
pp. 219-237
Author(s):  
Gal Porat-Dahlerbruch ◽  
Amir Goldbourt ◽  
Tatyana Polenova
Keyword(s):  
Lipid Bilayers ◽  
Magic Angle Spinning ◽  
Drug Binding ◽  
Mas Nmr ◽  
Atomic Resolution ◽  
Magic Angle ◽  
Experimental Conditions ◽  
Functional Studies ◽  
The Past ◽  
Angle Spinning

Techniques for atomic-resolution structural biology have evolved during the past several decades. Breakthroughs in instrumentation, sample preparation, and data analysis that occurred in the past decade have enabled characterization of viruses with an unprecedented level of detail. Here we review the recent advances in magic-angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy for structural analysis of viruses and viral assemblies. MAS NMR is a powerful method that yields information on 3D structures and dynamics in a broad range of experimental conditions. After a brief introduction, we discuss recent structural and functional studies of several viruses investigated with atomic resolution at various levels of structural organization, from individual domains of a membrane protein reconstituted into lipid bilayers to virus-like particles and intact viruses. We present examples of the unique information revealed by MAS NMR about drug binding, conduction mechanisms, interactions with cellular host factors, and DNA packaging in biologically relevant environments that are inaccessible by other methods.

scholarly journals Ellagitannin–Lipid Interaction by HR-MAS NMR Spectroscopy

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 373
Author(s):  
Valtteri Virtanen ◽  
Susanna Räikkönen ◽  
Elina Puljula ◽  
Maarit Karonen
Keyword(s):  
Nmr Spectroscopy ◽  
Lipid Bilayers ◽  
Membrane Lipids ◽  
Nuclear Overhauser Effect ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Relaxation Rates ◽  
Lipid Mixture ◽  
Nuclear Overhauser ◽  
Angle Spinning

Ellagitannins have antimicrobial activity, which might be related to their interactions with membrane lipids. We studied the interactions of 12 different ellagitannins and pentagalloylglucose with a lipid extract of Escherichia coli by high-resolution magic angle spinning NMR spectroscopy. The nuclear Overhauser effect was utilized to measure the cross relaxation rates between ellagitannin and lipid protons. The shifting of lipid signals in 1H NMR spectra of ellagitannin–lipid mixture due to ring current effect was also observed. The ellagitannins that showed interaction with lipids had clear structural similarities. All ellagitannins that had interactions with lipids had glucopyranose cores. In addition to the central polyol, the most important structural feature affecting the interaction seemed to be the structural flexibility of the ellagitannin. Even dimeric and trimeric ellagitannins could penetrate to the lipid bilayers if their structures were flexible with free galloyl and hexahydroxydiphenoyl groups.

scholarly journals Imidazole-imidazole hydrogen bonding in the pH sensing Histidine sidechains of Influenza A M2

2019 ◽  
Author(s):  
Kumar Tekwani Movellan ◽  
Melanie Wegstroth ◽  
Kerstin Overkamp ◽  
Andrei Leonov ◽  
Stefan Becker ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Influenza A ◽  
Chemical Shifts ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Ph Sensing ◽  
Quaternary Structures ◽  
Angle Spinning ◽  
Neutral Charge State ◽  
Hydrogen Bonded

ABSTRACTThe arrangement of histidine sidechains in influenza A M2 tetramer determines their pKa values, which define pH controlled proton conduction critical to the virus lifecycle. Both water associated and hydrogen bonded Imidazole–Imidazolium histidine quaternary structures have been proposed, based on crystal structures, and NMR chemical shifts, respectively. Here we show, using the conduction domain construct of M2 in lipid bilayers, that the imidazole rings are hydrogen bonded even at a pH of 7.8 in the neutral charge state.An intermolecular 8.9 ± 0.3 Hz 2hJNN hydrogen bond is observed between H37 Nε and Nδ recorded in a fully protonated sample with 100 kHz magic-angle spinning. This interaction could not be detected in the drug-bound sample.

scholarly journals Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers

2007 ◽  
Vol 35 (5) ◽  
pp. 991-995 ◽  
Author(s):  
C. Ader ◽  
R. Schneider ◽  
K. Seidel ◽  
M. Etzkorn ◽  
M. Baldus
Keyword(s):  
Nmr Spectroscopy ◽  
Small Molecules ◽  
Lipid Bilayers ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Domain Formation ◽  
Structure And Dynamics ◽  
Molecular Complexation ◽  
Angle Spinning ◽  
Insight Into

ssNMR (solid-state NMR) spectroscopy provides increasing possibilities to study the structural and dynamic aspects of biological membranes. Here, we review recent ssNMR experiments that are based on MAS (magic angle spinning) and that provide insight into the structure and dynamics of membrane systems at the atomic level. Such methods can be used to study membrane architecture, domain formation or molecular complexation in a way that is highly complementary to other biophysical methods such as imaging or calorimetry.

scholarly journals Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

2013 ◽  
Vol 394 (11) ◽  
pp. 1453-1463 ◽  
Author(s):  
Hoa Q. Do ◽  
Marc Wittlich ◽  
Julian M. Glück ◽  
Luis Möckel ◽  
Dieter Willbold ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Bilayers ◽  
Spin Diffusion ◽  
Magic Angle Spinning ◽  
Proton Spin ◽  
Phospholipid Bilayers ◽  
Amino Acid Type ◽  
Magic Angle ◽  
Amino Acid Residues ◽  
Angle Spinning

Abstract HIV-1 Vpu and CD4(372–433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13C and 15N isotopes, and separately reconstituted into phospholipid bilayers. Highly resolved dipolar cross-polarization (CP)-based solid-state NMR spectra of the two transmembrane proteins were recorded under magic angle sample spinning. Partial assignment of 13C resonances was achieved. Site-specific assignments were obtained for 13 amino acid residues of CD4(372–433) and two Vpu residues. Additional amino acid type-specific assignments were achieved for 10 amino acid spin systems for both CD4(372–433) and Vpu. Further, structural flexibility was probed with different dipolar recoupling techniques, and the correct insertion of the transmembrane domains into the lipid bilayers was confirmed by proton spin diffusion experiments.

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