Studies on the transmembrane domain of phospholamban using rotational resonance and Magic angle oriented sample spinning (MAOSS) NMR spectroscopy

1998 ◽  
Vol 26 (3) ◽  
pp. S194-S194 ◽  
Author(s):  
Z. AHMED ◽  
D. MIDDLETON ◽  
C. GLAUBITZ ◽  
A. WATTS
Keyword(s):  
Nmr Spectroscopy ◽  
Transmembrane Domain ◽  
Magic Angle ◽  
Oriented Sample ◽  
Rotational Resonance

scholarly journals Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers

2014 ◽  
Vol 112 (2) ◽  
pp. E119-E126 ◽  
Author(s):  
Nabanita Das ◽  
Jian Dai ◽  
Ivan Hung ◽  
Malini Rajagopalan ◽  
Huan-Xiang Zhou ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Mycobacterium Tuberculosis ◽  
Lipid Bilayers ◽  
Transmembrane Domain ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Transmembrane Helices ◽  
Oriented Sample ◽  
Angle Spinning ◽  
Dynamics Simulations

The 93-residue transmembrane protein CrgA in Mycobacterium tuberculosis is a central component of the divisome, a large macromolecular machine responsible for cell division. Through interactions with multiple other components including FtsZ, FtsQ, FtsI (PBPB), PBPA, and CwsA, CrgA facilitates the recruitment of the proteins essential for peptidoglycan synthesis to the divisome and stabilizes the divisome. CrgA is predicted to have two transmembrane helices. Here, the structure of CrgA was determined in a liquid–crystalline lipid bilayer environment by solid-state NMR spectroscopy. Oriented-sample data yielded orientational restraints, whereas magic-angle spinning data yielded interhelical distance restraints. These data define a complete structure for the transmembrane domain and provide rich information on the conformational ensembles of the partially disordered N-terminal region and interhelical loop. The structure of the transmembrane domain was refined using restrained molecular dynamics simulations in an all-atom representation of the same lipid bilayer environment as in the NMR samples. The two transmembrane helices form a left-handed packing arrangement with a crossing angle of 24° at the conserved Gly39 residue. This helix pair exposes other conserved glycine and alanine residues to the fatty acyl environment, which are potential sites for binding CrgA’s partners such as CwsA and FtsQ. This approach combining oriented-sample and magic-angle spinning NMR spectroscopy in native-like lipid bilayers with restrained molecular dynamics simulations represents a powerful tool for structural characterization of not only isolated membrane proteins, but their complexes, such as those that form macromolecular machines.

Wideline 2H -NMR Spectroscopy and Imaging of Solids

1994 ◽  
Vol 49 (1-2) ◽  
pp. 19-26 ◽  
Author(s):  
B. Blümich
Keyword(s):  
Nmr Spectroscopy ◽  
Excitation Power ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
2H Nmr ◽  
Stochastic Excitation ◽  
2H Nmr Spectroscopy ◽  
Spatially Inhomogeneous ◽  
Recent Developments ◽  
Angle Spinning

Abstract Recent developments, focussing on reduction of the rf excitation power by stochastic excitation, on improvements in sensitivity and excitation bandwidth by magic angle spinning, and on combining wideline spectroscopy with spatial resolution for investigations o f spatially inhomogeneous objects are reviewed.

scholarly journals Sampling Method Affects HR-MAS NMR Spectra of Healthy Caprine Brain Biopsies

Metabolites ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 38
Author(s):  
Annakatrin Häni ◽  
Gaëlle Diserens ◽  
Anna Oevermann ◽  
Peter Vermathen ◽  
Christina Precht
Keyword(s):  
Nmr Spectroscopy ◽  
Sampling Method ◽  
Magic Angle Spinning ◽  
Mas Nmr ◽  
Magic Angle ◽  
1H Nuclear Magnetic Resonance ◽  
Rapid Changes ◽  
Tissue Degradation ◽  
Angle Spinning

The metabolic profiling of tissue biopsies using high-resolution–magic angle spinning (HR-MAS) 1H nuclear magnetic resonance (NMR) spectroscopy may be influenced by experimental factors such as the sampling method. Therefore, we compared the effects of two different sampling methods on the metabolome of brain tissue obtained from the brainstem and thalamus of healthy goats by 1H HR-MAS NMR spectroscopy—in vivo-harvested biopsy by a minimally invasive stereotactic approach compared with postmortem-harvested sample by dissection with a scalpel. Lactate and creatine were elevated, and choline-containing compounds were altered in the postmortem compared to the in vivo-harvested samples, demonstrating rapid changes most likely due to sample ischemia. In addition, in the brainstem samples acetate and inositols, and in the thalamus samples ƴ-aminobutyric acid, were relatively increased postmortem, demonstrating regional differences in tissue degradation. In conclusion, in vivo-harvested brain biopsies show different metabolic alterations compared to postmortem-harvested samples, reflecting less tissue degradation. Sampling method and brain region should be taken into account in the analysis of metabolic profiles. To be as close as possible to the actual situation in the living individual, it is desirable to use brain samples obtained by stereotactic biopsy whenever possible.

Pulsed Field Gradient Selection in Two-Dimensional Magic Angle Spinning NMR Spectroscopy of Dipolar Solids

1998 ◽  
Vol 134 (2) ◽  
pp. 355-359 ◽  
Author(s):  
Tilo Fritzhanns ◽  
Siegfried Hafner ◽  
Dan E. Demco ◽  
Hans W. Spiess ◽  
Frank H. Laukien
Keyword(s):  
Nmr Spectroscopy ◽  
Field Gradient ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Two Dimensional ◽  
Pulsed Field ◽  
Angle Spinning
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