Researchers 'Watch' Protein Aggregation Process That Leads to Parkinson's Disease - Parkinson's News Today

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Researchers 'Watch' Protein Aggregation Process That Leads to Parkinson's Disease - Parkinson's News Today

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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

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d2D

PECAN

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RCI

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Chemical shifts:

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SAVES2 or SAVES4

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Methyl S2

B-factor

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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

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Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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12-02-2016, 07:45 AM

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Researchers 'Watch' Protein Aggregation Process That Leads to Parkinson's Disease - Parkinson's News Today

Researchers 'Watch' Protein Aggregation Process That Leads to Parkinson's Disease - Parkinson's News Today

Parkinson's News Today

Researchers 'Watch' Protein Aggregation Process That Leads to Parkinson's Disease
Parkinson's News Today
In the meantime, researchers could follow this â??unfoldingâ?? of the proteins using a technique called nuclear magnetic resonance (NMR) spectroscopy. NMR gave the team access to the folding and unfolding process so members could analyze these ...

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