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The sequence of PKN1 3 was appended to the database, and peptides were searched directly against that protein sequence.
This design enables new variables to be appended to the database as new datasets are loaded, without altering the underlying database schema.
Both interfaces also enable the curator to add new records so that new genes or new ortholog groups can be appended to the database.
Proteins were identified using the software's embedded ion accounting algorithm and a search of the Glycine max database with MassPREP digestion standards (MPDS) UniProtKB/Swiss-Prot sequences (Phosphorylase - P00489 - PHS2_RABIT, Bovine Hemoglobin - P02070 - HBB_BOVIN, ADH - P00330 - ADH1_YEAST, BSA - P02769 - ALBU_BOVIN) that were appended to the database.
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The databases were reversed "on-the fly" during the database query searches, and appended to the original database to assess the false positive rate of identification.
The growth equations and their computed standard-state free energy yields are appended to the thermodynamic database used in conventional geochemical reaction path modeling, providing a direct coupling between chemical species participating in both microbial growth and geochemical reactions.
Both the consensus sequences and the linked taxonomic information were then appended to the UNITE database files.
Reversed sequences of all proteins were appended to the protein database to assess the number of false positive peptide-spectrum matches (Elias and Gygi, 2007).
These novel protein sequences are then appended to the reference database and employed for MS-searching, enabling the detection of novel peptides.
Furthermore, randomized versions of the applied databases were appended to the original databases using the decoy perl script (Matrix Science, Boston, USA) downloadable at.
To determine false discovery rates (FDRs) of protein identification, both protein sequence databases were reversed and appended to the original databases as decoy sequences.
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