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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4214-4215 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 124 |
| Issue number | 16 |
| DOIs | |
| State | Published - Apr 24 2002 |
| Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry
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