Signal enhancement in protein NMR using the spin-noise tuning optimum.

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Signal enhancement in protein NMR using the spin-noise tuning optimum.

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NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

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Amber

Structure from chemical shifts:

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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Methyl S2

B-factor

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Shiftx2

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Proshift

PPM

CheShift-2- Cα

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Camcoil

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Disordered proteins:

MAXOCC

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Protein disorder:

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Protein solubility:

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10-07-2010, 10:33 AM

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Signal enhancement in protein NMR using the spin-noise tuning optimum.

Signal enhancement in protein NMR using the spin-noise tuning optimum.

Signal enhancement in protein NMR using the spin-noise tuning optimum.

J Biomol NMR. 2010 Oct 6;

Authors: Nausner M, Goger M, Bendet-Taicher E, Schlagnitweit J, Jerschow A, Müller N

We have assessed the potential of an alternative probe tuning strategy based on the spin-noise response for application in common high-resolution multi-dimensional biomolecular NMR experiments with water signal suppression on aqueous and salty samples. The method requires the adjustment of the optimal tuning condition, which may be offset by several 100*kHz from the conventional tuning settings using the noise response of the water protons as an indicator. Although the radio frequency-pulse durations are typically longer under such conditions, signal-to-noise gains of up to 22% were achieved. At salt concentrations up to 100*mM a substantial sensitivity gain was observed.

PMID: 20924647 [PubMed - as supplied by publisher]

Source: PubMed

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