Observation of conserved solution-phase secondary structure in gas-phase tryptic peptides.
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.
Ruotolo
Brandon T
BT
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.
Verbeck
Guido F
GF
Thomson
Lisa M
LM
Gillig
Kent J
KJ
Russell
David H
DH
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D005740:Gases; D006454:Hemoglobins / Q000737:chemistry*; D006736:Horses; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions
D005740:Gases; D006454:Hemoglobins; D009211:Myoglobin; D009842:Oligopeptides; D010446:Peptide Fragments; D012996:Solutions