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Investigation of Sequence-to-Structure Relationships in Peptides

The gas phase provides a simplified environment for the study of biomolecular structure; because solvent effects are absent, conformations are stabilized solely by intramolecular interactions. That is, peptide structure in vacuo should be defined solely by the peptide sequence. Thus far, we have approached the sequence/structure problem from two directions: studies of peptides produced from enzymatic digestion of common proteins and homopolymers. These studies are made possible by the nested ion mobility/time-of-flight approach, which allows us to measure cross sections for many peptides in a single experiment.
 

Relevant Publications:
Valentine, S. J.; Counterman, A. E.; Clemmer, D. E. A Database of 660 Peptide Ion Cross Sections: Use of Intrinsic Size Parameters for Bona Fide Predictions of Cross Sections, J. Am. Soc. Mass Spectrom. 1999, 10, 1188-1211.

Henderson, S. C.; Li, J.; Counterman, A. E.; Clemmer, D. E. Intrinsic Size Parameters for Val, Ile, Leu, Gln, Thr, Phe, and Trp Residues from Ion Mobility Measurements of Polyamino Acid Ions, J. Phys. Chem. B 1999, 103, 8780-8785.

Counterman, A. E.; Clemmer, D. E. Volumes of Individual Amino Acid Residues in Gas-Phase Peptide Ions, J. Am. Chem. Soc. 1999, 121, 4031-4039.

Valentine, S. J.; Counterman, A. E.; Hoaglund-Hyzer, C. S.; Clemmer, D. E. Intrinsic Amino Acid Size Parameters from a Series of 113 Lysine-Terminated Tryptic Digest Peptide Ions, J. Phys. Chem. B, 1999, 103, 1203-1207.