| MWexperimental | 91 | kDa |
| MWexpected | 181 | kDa |
| VPorod | 142 | nm3 |
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log I(s)
6.03×102
6.03×101
6.03×100
6.03×10-1
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s, nm-1
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Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects.
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z, J Biol Chem :101007 (2021) Europe PMCSASDL92 – Human acetylcholinesterase, covalently bound to paraoxon
acetylcholinesteraseacetylcholinesterase
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Fits and models
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Synchrotron SAXS
data from solutions of
Human acetylcholinesterase, covalently bound to paraoxon
in
50 mM Tris/HCl, 100 mM NaCl, pH 7.4
were collected
on the
BL4-2 beam line
at the Stanford Synchrotron Radiation Lightsource (SSRL) storage ring
(Menlo Park, CA, USA)
using a Rayonix MX225-HE detector
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 2.00 mg/ml was measured
at 22°C.
10 successive
1 second frames were collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The estimated experimental MW and shape of the PDDF indicate this sample represents a mixture of homodimer and monomer. X-ray wavelength: UNKNOWN. |
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