Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain - Nature.com

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Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain - Nature.com

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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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:

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NOEs, other restraints:

Chemical shifts:

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Pseudocontact shifts:

Protein geomtery:

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Backbone S2

Methyl S2

B-factor

Molecular dynamics:

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Chemical shifts prediction:

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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

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Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain - Nature.com

Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain - Nature.com

Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain Nature.com Read here

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