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• W2035156730 abstract "Abstract The use of electrospray ionization mass spectrometry (ESI‐MS) for studying non‐covalent interactions between macromolecules and ligands is well established. ESI‐MS can be a useful tool for the determination of dissociation constants between molecules in the gas phase. We validate this method by studying the binding of the catalytic domain of cellobiohydrolase I (CBH I) from Trichoderma reesei to the disaccharide inhibitor cellobiose. The method was further applied to study two newly synthesized cellobiose derivatives ( m ‐iodobenzyl 2‐deoxy‐2‐azido‐ β ‐cellobioside and p ‐benzyloxybenzyl β ‐cellobioside). In a titration experiment, peak areas of different charge states of the free enzyme and the complex were summed in order to determine the dissociation constant. For cellobiose and m ‐iodobenzyl 2‐deoxy‐2‐azido‐ β ‐cellobioside, the calculated values are in good agreement with those reported from either displacement titration or equilibrium binding experiments in solution. Due to non‐specific binding, the dissociation constant of p ‐benzyloxybenzyl β ‐cellobioside does not correspond with the solution‐based value. Our results indicate the need for careful interpretation of data sets when using nanoESI to study non‐covalent interactions. Copyright © 2004 John Wiley & Sons, Ltd." @default.
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• W2035156730 date "2004-11-15" @default.
• W2035156730 modified "2023-10-15" @default.
• W2035156730 title "Evaluation of automated nano-electrospray mass spectrometry in the determination of non-covalent protein-ligand complexes" @default.
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• W2035156730 doi "https://doi.org/10.1002/rcm.1728" @default.
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