scholarly journals Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution

2021 ◽  
Author(s):  
Morgane Callon ◽  
Alexander A. Malär ◽  
Sara Pfister ◽  
Václav Římal ◽  
Marco E. Weber ◽  
...  
Keyword(s):  
Magnetic Field ◽  
Solid State Nmr ◽  
Nmr Spectra ◽  
Superconducting Magnets ◽  
Molecular Machines ◽  
Side Chain ◽  
Proton Resonance Frequency ◽  
Proton Resonance ◽  
Viral Capsids ◽  
Large Panel

AbstractProgress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200 MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins, viral capsids, fibrils and large molecular assemblies. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in 13C spectra substantially higher numbers of peaks can be resolved compared to 850 MHz while for 1H spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.

scholarly journals Biomolecular solid-state NMR spectroscopy at highest field: the gain in resolution at 1200 MHz

2021 ◽  
Author(s):  
Morgane Calon ◽  
Alexander A Malar ◽  
Sara Pfister ◽  
Vaclav Rimal ◽  
Marco E Weber ◽  
...  
Keyword(s):  
Magnetic Field ◽  
Solid State Nmr ◽  
Nmr Spectra ◽  
Superconducting Magnets ◽  
Molecular Machines ◽  
Side Chain ◽  
Proton Resonance Frequency ◽  
Proton Resonance ◽  
Viral Capsids ◽  
Large Panel

Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200 MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins and viral capsids and others. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in 13C spectra substantially higher numbers of peaks can be resolved compared to 850 MHz while for 1H spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.

Thermosetting Mechanism Study of Organosilicon Polymer Containing Carborane by Solid-State NMR Spectroscopy

1999 ◽  
Vol 576 ◽  
Author(s):  
H. Kimura ◽  
K. Okita ◽  
M. Ichitani ◽  
M. Yonezawa ◽  
T. Sugimoto
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Spectra ◽  
Main Chain ◽  
Addition Reaction ◽  
Side Chain ◽  
Mechanism Study ◽  
Nmr Method ◽  
Organosilicon Polymer ◽  
Thermal Stable

ABSTRACTThe thermosetting mechanism of an organosilicon polymer containing carborane has been studied utilizing the 13and 29Si solid-state NMR method. The polymer having C≡C bonds in the main chain and CH═CH2, Si-H bonds, and carborane in the bulky side chain, shows a very highly thermal stability in air by curing. From 13C and 29Si NMR spectra of the polymer, it was found that the intermolecular cross-linking reactions of the polymer was due to (1) the diene reaction between Ph-C≡C and C≡C and (2) the addition reaction between side chain terminal and Ph-C≡C and between CH═CH2 and Si–H, and a very highly thermal stable structure is formed.

scholarly journals Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 752
Author(s):  
Evgeny Nimerovsky ◽  
Kumar Tekwani Movellan ◽  
Xizhou Cecily Zhang ◽  
Marcel C. Forster ◽  
Eszter Najbauer ◽  
...  
Keyword(s):  
Magnetic Field ◽  
Membrane Proteins ◽  
Superconducting Magnets ◽  
Magic Angle Spinning ◽  
Mas Nmr ◽  
Magic Angle ◽  
Proton Resonance Frequency ◽  
High Resolution Nmr ◽  
Homogeneous Broadening ◽  
Angle Spinning

The available magnetic field strength for high resolution NMR in persistent superconducting magnets has recently improved from 23.5 to 28 Tesla, increasing the proton resonance frequency from 1 to 1.2 GHz. For magic-angle spinning (MAS) NMR, this is expected to improve resolution, provided the sample preparation results in homogeneous broadening. We compare two-dimensional (2D) proton detected MAS NMR spectra of four membrane proteins at 950 and 1200 MHz. We find a consistent improvement in resolution that scales superlinearly with the increase in magnetic field for three of the four examples. In 3D and 4D spectra, which are now routinely acquired, this improvement indicates the ability to resolve at least 2 and 2.5 times as many signals, respectively.

Side Chain Resonances in Static Oriented Proton-Decoupled15N Solid-State NMR Spectra of Membrane Proteins

2009 ◽  
Vol 131 (18) ◽  
pp. 6340-6341 ◽  
Author(s):  
Christopher Aisenbrey ◽  
Lydia Prongidi-Fix ◽  
Alexandre Chenal ◽  
Daniel Gillet ◽  
Burkhard Bechinger
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Nmr Spectra ◽  
Side Chain

E-Homolupane Derivatives Substituted in Position 17 and 22a. 1H NMR, 13C NMR and IR Spectra

1995 ◽  
Vol 60 (4) ◽  
pp. 619-635 ◽  
Author(s):  
Václav Křeček ◽  
Stanislav Hilgard ◽  
Miloš Buděšínský ◽  
Alois Vystrčil
Keyword(s):  
Nmr Spectra ◽  
2D Nmr ◽  
Coupling Constants ◽  
Side Chain ◽  
Oxidation Reactions ◽  
H Nmr ◽  
Complete Assignment ◽  
Nmr Techniques ◽  
Intramolecular Association ◽  
C Nmr

A series of derivatives with various oxygen functionalities in positions 17,22a or 19,20 was prepared from diene I and olefin XVI by addition and oxidation reactions. The structure of the obtained compounds was confirmed by 1H NMR, 13C NMR and IR spectroscopy. The kind of intramolecular association of the 17α-hydroxy group was studied in connection with modification of the side chain and substitution in position 22a. Complete assignment of the hydrogen signals and most of the coupling constants was accomplished using a combination of 1D and 2D NMR techniques. The 1H and 13C NMR spectra are discussed.

Solid state NMR spectra of rapidly quenched superionic glasses composed of two lithium ortho-oxosalts

1996 ◽  
Vol 86-88 ◽  
pp. 535-538 ◽  
Author(s):  
Masanari Takahashi ◽  
Hiroshi Toyuki ◽  
Masahiro Tatsumisago ◽  
Tsutomu Minami
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Spectra
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