NMR paper An efficient fusion expression system for protein and peptide overexpression in Esche

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[NMR paper] An efficient fusion expression system for protein and peptide overexpression in Esche

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NMR processing:

MDD

NMR assignment:

Backbone:

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

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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11-24-2010, 09:01 PM

nmrlearner

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An efficient fusion expression system for protein and peptide overexpression in Esche

An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.

Related Articles An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.

Protein Pept Lett. 2003 Apr;10(2):175-81

Authors: Cheng Y, Liu D, Feng Y, Jing G

An efficient fusion expression system with a small fusion partner, His6-tagged N-terminal fragment of staphylococcal nuclease R, has been constructed and tested with two genes. The results show that the system is not only suitable for overexpression of small proteins and peptides but simplifies purification of target proteins and peptides. The study also provides a practical method for preparation of isotope-labeled protein sample for NMR analysis.

PMID: 12678815 [PubMed - indexed for MEDLINE]

Source: PubMed

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