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NMR processing:
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PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
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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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CS23D
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
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NMR model quality:
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iCing
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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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CH3shift- Methyl
ArShift- Aromatic
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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
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 01-26-2012, 12:10 AM
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Default Under the electron microscope -- A 3-D image of an individual protein - PhysOrg.com


PhysOrg.com


Under the electron microscope -- A 3-D image of an individual protein
PhysOrg.com
Scientists routinely create models of proteins using X-ray diffraction, nuclear magnetic resonance, and conventional cryo-electron microscope (cryoEM) imaging. But these models require computer â??averagingâ?? of data from analysis of thousands, ...
Under the electron microscope - a 3D image of an individual proteinNanowerk LLC

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Under the electron microscope -- A 3-D image of an individual protein - PhysOrg.com
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