NMR paper A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

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[NMR paper] A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

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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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Fragment-based:

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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

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PECAN

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RCI

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HADDOCK

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SAVES2 or SAVES4

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Methyl S2

B-factor

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Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

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Protein solubility:

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11-19-2010, 08:32 PM

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A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

Related Articles A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins.

J Biomol NMR. 2001 May;20(1):11-4

Authors: Zhou P, Lugovskoy AA, Wagner G

Protein-fusion constructs have been used with great success for enhancing expression of soluble recombinant protein and as tags for affinity purification. Unfortunately the most popular tags, such as GST and MBP, are large, which hinders direct NMR studies of the fusion proteins. Cleavage of the fusion proteins often re-introduces problems with solubility and stability. Here we describe the use of N-terminally fused protein G (B1 domain) as a non-cleavable solubility-enhancement tag (SET) for structure determination of a dimeric protein complex. The SET enhances the solubility and stability of the fusion product dramatically while not interacting directly with the protein of interest. This approach can be used for structural characterization of poorly behaving protein systems, and would be especially useful for structural genomics studies.

PMID: 11430750 [PubMed - indexed for MEDLINE]

Source: PubMed

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