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Ab initio:
GeNMR
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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UNIO Shiftinspector
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NMR model quality:
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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CH3shift- Methyl
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ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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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:
camLILA
ccSOL
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camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default The power, pitfalls and potential of the nanodisc system for NMR-based studies.

The power, pitfalls and potential of the nanodisc system for NMR-based studies.

Related Articles The power, pitfalls and potential of the nanodisc system for NMR-based studies.

Biol Chem. 2016 Jul 23;

Authors: Viegas A, Viennet T, Etzkorn M

Abstract
The choice of a suitable membrane mimicking environment is of fundamental importance for the characterization of structure and function of membrane proteins. In this respect, usage of the lipid bilayer nanodisc technology provides a unique potential for NMR-based studies. This review summarizes the recent advances in this field, focusing on (i) the strengths of the system, (ii) the bottlenecks that may be faced as well as (iii) promising capabilities that may be explored in future studies.


PMID: 27451995 [PubMed - as supplied by publisher]



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