While performing STD screening I noticed that I have signals in my difference spectras, that are constant accross all samples, also if there is no ligand and only protein.
The protein was purified via size exclusion and is in deuterated PBS.
Observing STD signals from a protein sample without a ligand suggests potential interactions with endogenous ligands, buffer components, contaminants, or conformational changes. These signals may arise from natural interactions within the sample or experimental conditions, and further investigation is needed to understand the specific binding events.
Are the signals from the protein itself or from something else?
The subtraction doesn't always remove the protein signals completely, and in that case you can use one of the pulse sequences that uses a spin lock to destroy the protein signals. On Bruker systems these are the std pulse sequences ending in .3
If the signals are from something else, you could try to run a cpmg experiment or similar to see what they might be.
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