scholarly journals Design of a single coil double resonance NMR probe for combined magic angle spinning double resonance experiments

1978 ◽  
Author(s):  
P.D. Murphy ◽  
B.C. Gerstein
Keyword(s):  
Double Resonance ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Single Coil ◽  
Angle Spinning

scholarly journals Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy

2015 ◽  
Vol 112 (47) ◽  
pp. 14611-14616 ◽  
Author(s):  
Si Yan ◽  
Changmiao Guo ◽  
Guangjin Hou ◽  
Huilan Zhang ◽  
Xingyu Lu ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Cell Biology ◽  
Double Resonance ◽  
Magic Angle Spinning ◽  
Atomic Resolution ◽  
Organelle Transport ◽  
Magic Angle ◽  
Associated Proteins ◽  
Angle Spinning ◽  
Resolution Structure

Microtubules and their associated proteins perform a broad array of essential physiological functions, including mitosis, polarization and differentiation, cell migration, and vesicle and organelle transport. As such, they have been extensively studied at multiple levels of resolution (e.g., from structural biology to cell biology). Despite these efforts, there remain significant gaps in our knowledge concerning how microtubule-binding proteins bind to microtubules, how dynamics connect different conformational states, and how these interactions and dynamics affect cellular processes. Structures of microtubule-associated proteins assembled on polymeric microtubules are not known at atomic resolution. Here, we report a structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain of dynactin motor on polymeric microtubules, solved by magic angle spinning NMR spectroscopy. We present the intermolecular interface of CAP-Gly with microtubules, derived by recording direct dipolar contacts between CAP-Gly and tubulin using double rotational echo double resonance (dREDOR)-filtered experiments. Our results indicate that the structure adopted by CAP-Gly varies, particularly around its loop regions, permitting its interaction with multiple binding partners and with the microtubules. To our knowledge, this study reports the first atomic-resolution structure of a microtubule-associated protein on polymeric microtubules. Our approach lays the foundation for atomic-resolution structural analysis of other microtubule-associated motors.

Recoupling of Heteronuclear Dipolar Interactions with Rotational-Echo Double-Resonance at High Magic-Angle Spinning Frequencies

2000 ◽  
Vol 146 (1) ◽  
pp. 132-139 ◽  
Author(s):  
Christopher P Jaroniec ◽  
Brett A Tounge ◽  
Chad M Rienstra ◽  
Judith Herzfeld ◽  
Robert G Griffin
Keyword(s):  
Double Resonance ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Dipolar Interactions ◽  
Rotational Echo Double Resonance ◽  
Angle Spinning

Magic angle spinning in solid state n.m.r. spectroscopy

1981 ◽  
Vol 299 (1452) ◽  
pp. 505-520 ◽  
Keyword(s):  
Double Resonance ◽  
Dipolar Interaction ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Dipolar Interactions ◽  
Basic Principles ◽  
Zeeman Field ◽  
Angle Spinning ◽  
Many Sources ◽  
Knight Shifts

Rapid specimen rotation about an axis inclined at the ‘magic angle’ of 54° 44' to the Zeeman field direction can remove many sources of broadening from the n.m.r. spectrum of a solid and enable finer features to be revealed. In this paper the basic principles of magic angle spinning are given and the effects on the chemical shift interaction, the magnetic dipolar and pseudo-dipolar interactions, both homonuclear and heteronuclear, and the electric quadrupolar interactions are examined. The anisotropic parts of these interactions are removed from the central spectrum and appear as spinning sidebands. The interactions that remain are the isotropic shifts and J couplings as in isotropic fluids. Examples of the effects of magic angle spinning on a variety of interactions are given. When applied to metals the anisotropy of Knight shift is removed, isotropic Knight shifts may be measured with precision, and the Ruderman-Kittel interaction may be determined in the presence of a much larger dipolar interaction. The effects of spinning on homogeneous and inhomogeneous spectra are distinguished. Sources of residual broadening are identified. Magic angle spinning may be used on its own, and may also be successfully combined with multiple-pulse and double resonance n.m.r. methods to obtain high-resolution n.m.r. spectra of powders and polymers.

scholarly journals Determination of Histidine Protonation States in Proteins by Fast Magic Angle Spinning NMR

2021 ◽  
Vol 8 ◽  
Author(s):  
Roman Zadorozhnyi ◽  
Sucharita Sarkar ◽  
Caitlin M. Quinn ◽  
Kaneil K. Zadrozny ◽  
Barbie K. Ganser-Pornillos ◽  
...  
Keyword(s):  
Metal Binding ◽  
Double Resonance ◽  
Imidazole Ring ◽  
Magic Angle Spinning ◽  
Proton Channel ◽  
Magic Angle ◽  
Ionization State ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

Histidine residues play important structural and functional roles in proteins, such as serving as metal-binding ligands, mediating enzyme catalysis, and modulating proton channel activity. Many of these activities are modulated by the ionization state of the imidazole ring. Here we present a fast MAS NMR approach for the determination of protonation and tautomeric states of His at frequencies of 40–62 kHz. The experiments combine 1H detection with selective magnetization inversion techniques and transferred echo double resonance (TEDOR)–based filters, in 2D heteronuclear correlation experiments. We illustrate this approach using microcrystalline assemblies of HIV-1 CACTD-SP1 protein.

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