Observation of conserved solution-phase secondary structure in gas-phase tryptic peptides. Academic Article uri icon


  • 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.

published proceedings

  • J Am Chem Soc

altmetric score

  • 3

author list (cited authors)

  • Ruotolo, B. T., Verbeck, G. F., Thomson, L. M., Gillig, K. J., & Russell, D. H.

citation count

  • 54

complete list of authors

  • Ruotolo, Brandon T||Verbeck, Guido F||Thomson, Lisa M||Gillig, Kent J||Russell, David H

publication date

  • April 2002