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Background binding was corrected using reactions containing no peptide.
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All measurements of binding were corrected using control dilution ITC experiments in which the nucleotide or MP265 was injected into appropriate buffer alone.
The binding energy was corrected using C(1s) at 284.6 eV.
The peak shift due to charge compensation was corrected using the binding energy of C1s peak.
Multiple testing was corrected using Bonferroni correction.
The shift of the binding energy due to the relative surface charging was corrected using the C 1s level at 284.8 eV as an internal standard.
The background was corrected using the Shirley method, and the binding energy of the C 1s peak from the support at 284.5 eV was taken as an internal standard.
Attenuation was corrected using CT images.
Attenuation was corrected using transmissive images.
In order to remove charging shifts and deal with Fermi edge coupling problems, binding energies were corrected using the peak of the C- C, H) C- Conent coming from contamination carbon (set to 284.6 eV).
All XPS data were corrected using the binding energy of C-C at 284.6 eV.
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