NMR paper Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions

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[NMR paper] Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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HADDOCK

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SAVES2 or SAVES4

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Methyl S2

B-factor

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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

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Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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10-15-2024, 11:40 PM

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Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions

Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions

Dynamic nuclear polarization (DNP) enhanced magic angle spinning (MAS) solid-state NMR carried out at 25 K enables rapid acquisition of multi-dimensional ^(13)C-^(15)N correlation spectra for protein structure studies and resonance assignment. Under commonly used DNP conditions, solvent deuteration reduces ¹H-^(15)N cross polarization (CP) efficiencies, necessitates more careful optimization, and requires longer high-power ^(15)N radio-frequency pulses. The sensitivity of 2D heteronuclear...

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