NMR paper Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

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[NMR paper] Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

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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

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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

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NOEs, other restraints:

Chemical shifts:

RDCs:

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SAVES2 or SAVES4

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FANDAS

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V-NMR

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Backbone S2

Methyl S2

B-factor

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Shiftx2

Sparta+

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

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08-21-2010, 11:04 PM

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Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 bet

Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.

Related Articles Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.

Science. 1990 Jul 27;249(4967):411-4

Authors: Kay LE, Clore GM, Bax A, Gronenborn AM

A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional carbon-13--nitrogen-15 (13C-15N)--edited nuclear Overhauser effect (NOE) spectroscopy to interleukin-1 beta, a protein of 153 residues. The NOEs between NH and aliphatic protons are first spread out into a third dimension by the 15N chemical shift of the amide 15N atom and subsequently into a fourth dimension by the 13C chemical shift of the directly bonded 13C atoms. By this means ambiguities in the assignment of NOEs between NH and aliphatic protons that are still present in the three-dimensional 15N-edited NOE spectrum due to extensive chemical shift overlap and degeneracy of aliphatic resonances are completely removed. Consequently, many more approximate interproton distance restraints can be obtained from the NOE data than was heretofore possible, thereby expanding the horizons of three-dimensional structure determination by NMR to larger proteins.

PMID: 2377896 [PubMed - indexed for MEDLINE]

Source: PubMed

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