Combinatorial libraries of synthetic peptides as a model for shotgun proteomics.

ABSTRACT: A synthetic approach to model the analytical complexity of biological proteolytic digests has been developed. Combinatorial peptide libraries ranging in length between 9 and 12 amino acids that represent typical tryptic digests were designed, synthesized, and analyzed. Individual libraries and mixtures thereof were studied by replicate liquid chromatography-ion trap mass spectrometry and compared to a tryptic digest of Deinococcus radiodurans. Similar to complex proteome analysis, replicate study of individual libraries identified additional unique peptides. Fewer novel sequences were revealed with each additional analysis in a manner similar to that observed for biological data. Our results demonstrate a bimodal distribution of peptides sorting to either very low or very high levels of de

SUBMITTER: Bohrer BC 

PROVIDER: S-EPMC2927099 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature