NMR paper PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic p

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[NMR paper] PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic p

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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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11-17-2010, 11:15 PM

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PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic p

PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins.

Related Articles PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins.

J Magn Reson. 1998 Sep;134(1):154-7

Authors: Bondon A, Mouro C

A new method for NMR spectra acquisition of paramagnetic proteins is described, based on the simple use of homonuclear broadband decoupling of the diamagnetic region. Several advantages are associated with this method which was applied to one-dimensional spectra, to 1D NOE-difference spectroscopy, and to 2D NOESY. The main advantage is a very flat baseline obtained using the PASE (paramagnetic signals enhancement) method. Furthermore, the bulky region of the diamagnetic protons being suppressed, clean NOE-difference spectra can be acquired as well as improved 2D NOESY maps. Applications on 1D 1H spectrum of bovine liver catalase (MW 230,000), and 1D and 2D on the high-spin form of the myoglobin, used as a model protein, are presented.

PMID: 9740741 [PubMed - indexed for MEDLINE]

Source: PubMed

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