[Question from NMRWiki Q&A forum] How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
we have done HSQC gradient titration with targeted proteins , most of cross peaks we observed intensity drop , 30 out of 95 peaks ( 70 percent intensity drop of each cross peak ) , other cross peaks also we observe intensity drop less than 70 percent , we did n"t observe any chemical shift change .( May be it is due to intermediate exchange regime of complex ) .ITC experiment showing 12uM binding constant .AUC experiment result is complex size 33 kd .
is their any method to extract residue information from intensity drop of HSQC titration spectra more specifically ?
How to minimize line broadening effect while taking HSQC Titration ?
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[Question from NMRWiki Q&A forum] Line broadening in nmr
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Hello can some body help me in understanding the line broadening effect in NMR? I am working with protein and small molecules and I observed severe broadening at a protein to ligand ratio 1:20. I am pretty sure that its not aggregation since i have the free ligand spectrum without the protein which didnt showed any broadening effect.
Hope somebody will guide me..
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