Bäumlisberger D, Kurz C, Rohmer M, Arrey TN, Schiller C, Moehring T, Möller WA, Karas M.
ASMS 2012 Poster
Besides being the main site of adenosine triphosphate (ATP), mitochondria are associated with a range of other processes and diseases such as cell growth, cellular
differentiation, mitochondrial disorder, aging processes and cardiac dysfunctions. To
obtain a better understanding of these mitochondrial processes and diseases, we
need to identify the proteins and proteins modifications involved.
The ability to identify and characterize large numbers of proteins from medium- to
high- complexity samples has made mass spectrometry (MS) coupled to reversedphase
high-performance liquid chromatography (HPLC) a common analytical technique in proteomics. Usually, the extracted proteins are digested with a suitable protease and the resulting peptide mixture is separated and analyzed. Trypsin is the common enzyme of choice for proteomics experiments. Digestion with trypsin (or any
single enzyme in general) often results in the identification of large numbers of
proteins, but sequence coverage is frequently incomplete. If maximum sequence
coverage is desired (e.g. when studying changes in protein modification or different
isoforms), then signals covering all or most of the protein sequence are needed.
Different approaches have been used to improve protein sequence coverage in
proteomics. In this study, data obtained from individual trypsin, chymotrypsin and
elastase digests.
Thermo Fisher Scientific
United States
