NMR paper Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia

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[NMR paper] Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia

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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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08-22-2010, 03:03 PM

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Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia

Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.

Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.

J Biomol NMR. 1997 Apr;9(3):299-305

Authors: Salgado J, Kalverda AP, Canters GW

The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through the electron self-exchange reaction in partially oxidised samples, and can be used for the selective detectionof protons around the metal. Relaxation-selective NMR pulse sequences, like super-WEFTand WEFT-NOESY, are used to achieve the desired selection of the signals. The spectraobtained show well-resolved signals corresponding to protons within a radius of approximately 7 A from the metal, including almost all protons from the coordinated residues. A significant increasein resolution as well as selection of the most relevant part of the protein (close to the activecentre) are the principal advantages of this technique, which can be used to obtain specificinformation about the metal site in blue copper proteins, to assist in the assignment of theirNMR spectra and to determine functional properties like the electron self-exchange rate.

PMID: 20680661 [PubMed - in process]

Source: PubMed

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