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The apparent deficiency in heme binding of these variants was further characterized by examining their visible electronic spectra, which more closely resembled that of free heme than that of hemoprotein.
Binding of these variants to receptors expressed on whole cells was analyzed by radioligand binding assays and correlated to their biological activities.
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Because of the apparent weak binding for these variants, they were deemed unsuitable for performing transfer assays.
We therefore predict a mild destabilization of the T-state as a consequence of the Leu or Cys replacement that might slightly increase the oxygen binding affinity of these variants.
Structural differences between Variant FS and wild type are also reflected in the loss of binding of the variant to FcγRII and FcγRIII receptors.
The decreased silencing activity of 5'-isomiR-101 5'-isomiR-101 5'-isomiR-101ding of this vagrees to Ago2 complexes.
To understand the impact of this important class of variants and to uncover new principles of BRCT phosphopeptide interactions, we have studied each of these six variants using a quantitative fluorescence polarization assay to determine the precise effect on peptide binding of each of these variants.
We hypothesize that measurement of the Km of cofactor binding in these variants would should no significant difference to the normal (WT) enzyme.
No evidence for binding or structural protection of these variants was identified in HX MS experiments, ruling out the potential for false contributions to GGCX deuterium uptake patterns.
(D) The binding of Sdo1p variants to the mature 60S subunit examined by co-sedimentation assay.
(E) The binding of Sdo1p variants to the mature 60S subunit examined by Bio-layer interferometry.
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