Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields

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Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields

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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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04-01-2011, 09:23 AM

nmrlearner

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Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields

Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields

Abstract Sensitive 2D solid-state 13Câ??13C correlation spectra of amyloid Î² fibrils have been recorded at very fast spinning frequencies and very high magnetic fields. It is demonstrated that PARIS-xy recoupling using moderate rf amplitudes can provide structural information by promoting efficient magnetization transfer even under such challenging experimental conditions. Furthermore, it has been shown both experimentally and by numerical simulations that the method is not very sensitive to dipolar truncation effects and can reveal direct transfer across distances of about 3.5â??4Ã?.

Content Type Journal Article
Pages 1-8
DOI 10.1007/s10858-011-9501-9
Authors
- Markus Weingarth, DÃ©partement de Chimie, Ecole Normale SupÃ©rieure, 24 rue Lhomond, 75231 Paris, France
- Yuichi Masuda, Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, 606-8502 Japan
- K. Takegoshi, Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, 606-8502 Japan
- Geoffrey Bodenhausen, DÃ©partement de Chimie, Ecole Normale SupÃ©rieure, 24 rue Lhomond, 75231 Paris, France
- Piotr Tekely, DÃ©partement de Chimie, Ecole Normale SupÃ©rieure, 24 rue Lhomond, 75231 Paris, France

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

Source: Journal of Biomolecular NMR

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