Magic Angle Spinning Nmr
Magic Angle Spinning Nmr - Related Videos
07:33
Magnetic Resonance Spectroscopy of live Drosophila melanogaster using Magic Angle Spinning
0 Views •
Cited by 5 •
2010
This technique enables the use of high-resolution magic angle spinning proton MR spectroscopy (HRMAS 1H-MRS) for molecular characterization of live Drosophila melanogaster with a conventional 14.1 tesla spectrometer equipped with an HRMAS probe.
08:55
High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
0 Views •
Cited by 11 •
2020
The molecular structures and dynamics of solids, liquids, gases, and mixtures are of critical interest to diverse scientific fields. High-temperature, high-pressure in situ MAS NMR enables detection of the chemical environment of constituents in mixed phase systems under tightly controlled chemical environments.
01:08
NMR Spectroscopy: Spin–Spin Coupling
0 Views •
2024
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
06:42
Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
0 Views •
Cited by 15 •
2020
Presented here is a protocol for cryogenic transfer of frozen samples into the dynamic nuclear polarization (DNP) magic angle spinning (MAS) nuclear magnetic resonance (NMR) probe. The protocol includes directions for rotor storage prior to the experiment and directions for viability measurements before and after the experiment.
11:44
Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
0 Views •
Cited by 4 •
2016
A detailed protocol describing the SSTD NMR method is presented here to help new users apply this new method to obtain the kinetic parameters of their own systems undergoing chemical exchange.
FAQs
This angle is chosen relative to the magnetic field because it averages orientation-dependent interactions during rapid sample rotation. In particular, chemical-shift anisotropy and dipolar couplings become less prominent in the measured signals, reducing line broadening. The resulting narrower signals make structural and dynamic features of solid biological samples more informative at the atomic scale.
Rapid rotation changes the orientation of the packed material continuously relative to the magnetic field. That motion averages interactions whose effects depend on molecular orientation, especially chemical-shift anisotropy and dipolar couplings. By decreasing their contribution to signal broadening, the technique produces narrower resonances that can reveal molecular conformation, interactions, and dynamics more clearly.
The method is suited to nonliquid biological materials that do not readily provide the information needed in solution studies. Membrane proteins, amyloid fibrils, protein complexes, and other assemblies can retain their relevant solid or assembled states during analysis. This expands structural investigation to systems whose organization or physical form makes solution characterization challenging.
The signals can support atomic-scale characterization of molecular conformation, interactions, and dynamics. Conformation refers to how a molecule is arranged in space, while interactions describe contacts or associations within a biological system. Examining these features helps researchers investigate how membrane proteins, fibrils, complexes, and related assemblies are organized and behave.
A nonliquid biological material is packed as the sample and positioned in a magnetic field. The sample is then rapidly rotated at approximately 54.74° relative to that field while nuclear magnetic resonance signals are recorded. Signal narrowing produced by the rotation supports subsequent interpretation of structural and dynamic features in the material.
Important applications include membrane proteins, amyloid fibrils, protein complexes, and other biological assemblies that are difficult to study in solution. These systems represent distinct structural contexts, from proteins associated with membranes to aggregated or interacting molecules. Studying them in their nonliquid forms can provide information that complements investigations of more accessible biological samples.
By characterizing conformation, interactions, and dynamics at atomic scale, the method can help connect molecular structure with biological behavior in disease-relevant assemblies. Amyloid fibrils and protein complexes are especially relevant examples from the biological applications described. The resulting structural information supports research into how such systems form, interact, or contribute to disease mechanisms.