![]() ![]() ![]() The influence of each amino acid on the observed cross section of the peptide has been quantified in terms of an intrinsic size parameter by solving for a system of equations that relates the frequency of the amino acid to measured cross section for different peptide sequences in the array of data. Analysis of these related peptide sequences has shown that there are correlations of measure cross section with the amino acid composition. As the cross section can provide valuable information about the three-dimensional structure of the ions, a large and actively updated collection of these measurements should benefit efforts to understand the intrinsic structural properties of these peptides in the absence of solvent and perhaps illuminate factors that influence folding.įrom the original database containing nearly 700 different peptide ions, a subset of more than 100 lysine-terminated peptide sequences that do not contain additional Lys, Arg, His, or Cys was created. Prior to the completion of this database, cross sections for only a few dozen peptides had been reported. ![]() This has allowed for the creation of a database of nearly 3000 singly and doubly charged peptide ions obtained from the tryptic digestion of common proteins. We have developed an instrumental-based method for quickly determining average cross sections for components of complex mixtures of peptides or digests of large proteins. For the purposes of this discussion, a prediction is considered to be accurate if it falls within 2% of the experimental values, as this is often the level of accuracy reported for ion mobility measurements of cross section. A method for accurate prediction of cross sections would be valuable. Consider, for example, five-residue tryptic fragments containing a C-terminal arginine or lysine residue there will be 320,000 different sequences. Despite the recent advancements in technology and chemical instrumentation, it is not yet feasible to measure cross sections for all sequences of small peptides. ![]()
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