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NMR processing:
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Side-chains:
UNIO ATNOS-Ascan
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UNIO ATNOS-Candid
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ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
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UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
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GeNMR
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Refinement:
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Structure from chemical shifts:
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CS23D
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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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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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Pseudocontact shifts:
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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ShiftS
Proshift
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
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camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 04-24-2013, 09:48 PM
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Default Team Effort - R&D Magazine - R & D Magazine


R & D Magazine


Team Effort - R&D Magazine
R & D Magazine
To achieve the best understanding of protein structure, researchers often look to nuclear magnetic resonance (NMR) and X-ray diffraction (XRD) techniques. High-powered X-rays have led to a host of fundamental discoveries in biology. However, the ...



Team Effort - R&D Magazine - R & D Magazine
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