Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Elite
ORGANISM(S): Schizosaccharomyces Pombe Oy26
SUBMITTER: Therese Dau
LAB HEAD: Juri Rappsilber
PROVIDER: PXD017321 | Pride | 2021-06-07
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
._Pombe_AspN-trypsin_rep1.raw | Raw | |||
._Pombe_AspN-trypsin_rep2.raw | Raw | |||
._Pombe_AspN-trypsin_rep2.zip | Other | |||
._Pombe_AspN-trypsin_rep3.raw | Raw | |||
._Pombe_AspN-trypsin_rep3.zip | Other |
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Analytical chemistry 20200706 14
Trypsin is the most used enzyme in proteomics. Nevertheless, proteases with complementary cleavage specificity have been applied in special circumstances. In this work, we analyzed the characteristics of five protease alternatives to trypsin for protein identification and sequence coverage when applied to <i>S. pombe</i> whole cell lysates. The specificity of the protease heavily impacted the number of proteins identified. Proteases with higher specificity led to the identification of more prote ...[more]