NMR paper Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization

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[NMR paper] Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization

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MDD

NMR assignment:

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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

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RCI

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HADDOCK

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SAVES2 or SAVES4

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FANDAS

MestReS

V-NMR

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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

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Shifty

Camcoil

Poulsen_rc_CS

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MAXOCC

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Protein solubility:

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03-16-2013, 02:22 AM

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Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization

Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization

Available online 14 March 2013
Publication year: 2013
Source:Journal of Magnetic Resonance

Robust and efficient band-selective magnetization transfer between CO and CA spins can be achieved in highly deuterated solid proteins by dipolar-based homonuclear cross polarization. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields where the isotropic chemical shift difference of CO and CA considerably exceeds the spinning rate. The most efficient recoupling is achieved when the sum of effective radio-frequency fields on CO and CA resonances equals two times the spinning rate. This method can be directly implemented in proton-detected versions of inter-residual correlation experiments as needed for resonance assignment in protein solid-state NMR spectroscopy.
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