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NMR processing:
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Ab initio:
GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Chemical shifts re-referencing:
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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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:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Old 04-11-2024, 09:29 AM
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Default Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)

Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)

ATP-hydrolysis-associated conformational change of the ?-subunit during the rotation of F(1)-ATPase (F(1)) has been discussed using cryo-electron microscopy (cryo-EM). Since it is worthwhile to further investigate the conformation of ATP at the catalytic subunit through an alternative approach, the structure of ATP bound to the F(1)?-subunit monomer (?) was analyzed by solid-state NMR. The adenosine conformation of ATP-? was similar to that of ATP analog in F(1) crystal structures. ^(31)P...

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