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Side-chains:
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Ab initio:
GeNMR
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UNIO ATNOS-Candid
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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:
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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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
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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:
Shiftx2
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
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
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Isotope labeling:
UPLABEL
Solid-state NMR:
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Default Structures, Dynamics, and Functions of Viral Membrane Proteins by NMR

Structures, Dynamics, and Functions of Viral Membrane Proteins by NMR

Publication date: 2 February 2018
Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1

Author(s): Luis G. Basso, Sang H. Park, Antonio J. Costa-Filho, Stanley J. Opella









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