NMR paper Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

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[NMR paper] Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

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NMR processing:

MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

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Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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FANDAS

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V-NMR

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ArShift- Aromatic

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Proshift

PPM

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Camcoil

Poulsen_rc_CS

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NMR sample preparation:

Protein disorder:

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Protein solubility:

Isotope labeling:

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11-10-2017, 05:01 PM

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Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

Related Articles Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.

J Biomol NMR. 2017 Nov 08;:

Authors: Wiegand T, Liao WC, Ong TC, Däpp A, Cadalbert R, Copéret C, Böckmann A, Meier BH

Abstract
DNP (dynamic nuclear polarization)-enhanced solid-state NMR is employed to directly detect protein-DNA and protein-ATP interactions and identify the residue type establishing the intermolecular contacts. While conventional solid-state NMR can detect protein-DNA interactions in large oligomeric protein assemblies in favorable cases, it typically suffers from low signal-to-noise ratios. We show here, for the oligomeric DnaB helicase from Helicobacter pylori complexed with ADP and single-stranded DNA, that this limitation can be overcome by using DNP-enhanced spectroscopy. Interactions are established by DNP-enhanced (31)P-(13)C polarization-transfer experiments followed by the recording of a 2D (13)C-(13)C correlation experiment. The NMR spectra were obtained in less than 2 days and allowed the identification of residues of the motor protein involved in nucleotide binding.

PMID: 29119516 [PubMed - as supplied by publisher]

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