Simultaneous acquisition of PAR and PAIN spectra

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Simultaneous acquisition of PAR and PAIN spectra

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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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03-03-2012, 01:39 AM

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Simultaneous acquisition of PAR and PAIN spectra

Simultaneous acquisition of PAR and PAIN spectra

Abstract We present a scheme that allows the simultaneous detection of PAR and PAIN correlation spectra in a single two-dimensional experiment. For both spectra, we obtain almost the same signal-to-noise ratio as if a PAR or PAIN spectrum is recorded separately, which in turn implies that one of the spectra may be considered additional information for free. The experiment is based on the observation that in a PAIN experiment, the PAR condition is always also fulfilled. The performance is demonstrated experimentally using uniformly 13C,15N-labeled samples of Nâ??fâ??MLFâ??OH and ubiquitin.

Content Type Journal Article
Category Communication
Pages 1-6
DOI 10.1007/s10858-012-9616-7
Authors
- Anders B. Nielsen, Physical Chemistry, ETH ZÃ¼rich, Wolfgang-Pauli-Strasse 10, 8093 ZÃ¼rich, Switzerland
- Kathrin SzÃ©kely, Physical Chemistry, ETH ZÃ¼rich, Wolfgang-Pauli-Strasse 10, 8093 ZÃ¼rich, Switzerland
- Julia Gath, Physical Chemistry, ETH ZÃ¼rich, Wolfgang-Pauli-Strasse 10, 8093 ZÃ¼rich, Switzerland
- Matthias Ernst, Physical Chemistry, ETH ZÃ¼rich, Wolfgang-Pauli-Strasse 10, 8093 ZÃ¼rich, Switzerland
- Niels Chr. Nielsen, Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, Center for Insoluble Protein Structures (inSPIN), University of Aarhus, 8000 Aarhus C, Denmark
- Beat H. Meier, Physical Chemistry, ETH ZÃ¼rich, Wolfgang-Pauli-Strasse 10, 8093 ZÃ¼rich, Switzerland

- Journal Journal of Biomolecular NMR
- Online ISSN 1573-5001
- Print ISSN 0925-2738

Source: Journal of Biomolecular NMR

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