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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
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UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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TALOS
MICS caps, β-turns
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
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NMR model quality:
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iCing
RDCs:
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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:
Shiftx2
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ArShift- Aromatic
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Proshift
PPM
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From sequence:
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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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Old 11-24-2010, 09:16 PM
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Default Dissection of heteronuclear NMR experiments for studies of magnetization transfer eff

Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.

Related Articles Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.

J Magn Reson. 2003 Nov;165(1):89-94

Authors: Braun D, Wüthrich K, Wider G

Modern NMR experiments for applications with biological macromolecules in solution typically include multiple magnetization transfer steps. When working with large structures, a significant fraction of the magnetization is lost during these transfers. For the design and optimization of complex experimental schemes, the magnetization transfer efficiencies have therefore commonly been calculated from the spin relaxation times. This paper now suggests a new method for measurement of individual transfer efficiencies directly with the system of interest, using short, reliable experiments. Initial applications of this approach with a 110,000 Da protein indicate that there is a wide range of transfer efficiencies among individual spin pairs in a structure of this size, which leads to a correspondingly large variation of the individual signal intensities and the need for techniques to enhance the weak signals.

PMID: 14568519 [PubMed - indexed for MEDLINE]



Source: PubMed
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