Abstract
Results from ion mobility studies of tryptic peptides suggest that, in some cases, the gas-phase structures can be related to the solution-phase structure of the parent protein. The interpretation of ion mobility measurements is supported by results from molecular modeling and H/D exchange experiments on the same peptides. This study clearly illustrates the utility of IM-MS for screening complex mixtures for peptides having intrinsically stable secondary/tertiary structures, and/or posttranslational modification.
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