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NMR processing:
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NMR assignment:
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MARS
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PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
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Chemical shifts:
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iCing
RDCs:
DC
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Pseudocontact shifts:
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Protein geomtery:
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PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
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MetaMQAPII
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STAN
Ramachandran Plot
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ERRAT
Verify_3D
Harmony
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
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Camshift
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
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default An in vitro kinetic assay of ATPase by phosphorus-31 NMR.

An in vitro kinetic assay of ATPase by phosphorus-31 NMR.

Related Articles An in vitro kinetic assay of ATPase by phosphorus-31 NMR.

Kurume Med J. 1990;37(3):153-7

Authors: Chinami M, Shingu M

The ATPase activity of RecA protein was examined by monitoring the changes of NMR phosphorus signals of ATP, ADP and inorganic phosphate. The areas of phosphorus-31 NMR peaks from inorganic phosphate and ADP, which increased with time, and the signals from ATP, which decreased with time, were fitted by a linear least square method to obtain the initial rate constants. The rate constants were examined for dependence on RecA protein concentration, temperature and pH. This assay system is useful for testing extrinsic physico-chemical effects on ATPase activity; because only essential components are present in a confined system, and the rate constants can be measured with a single step.

PMID: 2149400 [PubMed - indexed for MEDLINE]



Source: PubMed
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