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Enhancing Sequence Coverage in Proteomics Studies by Using a Combination of Proteolytic Enzymes

Reputable Mentor II
Reputable Mentor II
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
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‎10-15-2021 04:48 AM
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