NMR paper Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR

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[NMR paper] Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR

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MDD

NMR assignment:

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NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

Structure from chemical shifts:

Fragment-based:

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Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

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TALOS

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d2D

PECAN

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Methyl S2

B-factor

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ArShift- Aromatic

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Proshift

PPM

CheShift-2- Cα

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Shifty

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Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

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NMR sample preparation:

Protein disorder:

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Protein solubility:

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02-26-2024, 09:15 PM

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Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR

Protein deuteration via algal amino acids to circumvent proton back-exchange for (1)H-detected solid-state NMR

With perdeuteration, solid-state NMR spectroscopy of large proteins suffers from incomplete amide-proton back-exchange. Using a 72 kDa micro-crystalline protein, we show that deuteration exclusively via deuterated amino acids, well-established in solution to suppress sidechain protonation without proton back-exchange obstacles, provides spectral resolution comparable to perdeuterated preparations at intermediate spinning frequencies.

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