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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
UNIO Candid
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
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Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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CheckShift
RefDB
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Pseudocontact shifts:
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What-If
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SAVES2 or SAVES4
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Verify_3D
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V-NMR
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Methyl S2
B-factor
Molecular dynamics:
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From structure:
Shiftx2
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ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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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:
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Default Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR

Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR spectroscopy.

Related Articles Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR spectroscopy.

J Biol Chem. 1993 Apr 15;268(11):7763-7

Authors: Lal S, Szwergold BS, Kappler F, Brown T

Recently we have identified two novel phosphorylated metabolites in the lenses of diabetic rats as sorbitol 3-phosphate (Sor-3-P) and fructose 3-phosphate (Fru-3-P). The latter compound is of particular interest since it is a potent glycating agent, which could account, at least in part, for the increased protein cross-linking and cataract formation in the lens of the diabetic rat. In order to gain insight into the mechanism of formation of these compounds, 31P NMR spectra of rat, pig, and rabbit lenses, perfused with media supplemented with glucose, fructose, or sorbitol, were acquired. Perfusion with fructose-supplemented media resulted in the production of Fru-3-P in all three species. This compound was not produced upon perfusion with fructose-deficient media. The identification of the newly synthesized material as Fru-3-P was confirmed by spiking perchloric acid extracts of the perfused lenses with synthetic Fru-3-P. Our results provide strong evidence for the existence of a fructose-3-phosphokinase in mammalian lenses. If this enzyme is present in human lenses as well, it will reinforce the hypothesis that this enzyme and its product, Fru-3-P, may play a role in diabetic cataractogenesis and that lenticular fructose-3-phosphokinase may provide another therapeutic target in the prevention and alleviation of diabetic cataracts.

PMID: 8385119 [PubMed - indexed for MEDLINE]



Source: PubMed
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