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NMR processing:
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Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
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PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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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:
Shiftx2
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PPM
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From sequence:
Shifty
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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:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.

Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.

Related Articles Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.

J Am Chem Soc. 2004 Nov 10;126(44):14377-9

Authors: Feng L, Orlando R, Prestegard JH

Application of nuclear magnetic resonance (NMR) methods for the structural characterization to larger and more complex protein systems can be facilitated through the development of new methods for resonance assignment. Here, a novel approach that relies on integration of NMR and mass spectrometry (MS) methods is explored. The approach relies on the fact that both NMR and MS are able to monitor rates of exchange of amide protons for water deuterons. Correlating the rates can connect cross-peak positions from NMR data with fragment masses from MS data to support sequential assignment. The example provided is for a small model protein, ubiquitin, but the potential for application to large, more difficult to express proteins is clear.

PMID: 15521756 [PubMed - indexed for MEDLINE]



Source: PubMed
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