AI Article Synopsis
- Proteomics has gained significance in recent decades, with a focus on identifying intact proteins, primarily using high-resolution mass spectrometry, leading to challenges in low-resolution methods.
- Our study explored a combined method using collision-induced dissociation (CID) and electron transfer without dissociation (ETnoD) to identify intact proteins, specifically testing with myoglobin.
- We developed a protocol called CID/ETnoD that enables sequence identification and validation of multiple intact proteins by generating stable product ions and analyzing them through multistage activation.
Article Abstract
Over the past decades, proteomics has become increasingly important and a heavily discussed topic. The identification of intact proteins remains a major focus in this field. While most intact proteins are analyzed using high-resolution mass spectrometry, identifying them through low-resolution mass spectrometry continues to pose challenges. In our study, we investigated the capability of identifying various intact proteins using collision-induced dissociation (CID) and electron transfer without dissociation (ETnoD). Using myoglobin as our test protein, stable product ions were generated with CID, and the identities of the product ions were identified with ETnoD. ETnoD uses a short activation time (AcT, 5 ms) to create sequential charge-reduced precursor ion (CRI). The charges of the fragments and their sequences were determined with corresponding CRI. The product ions can be selected for subsequent CID (termed CID) combined with ETnoD for further sequence identification and validation. We refer to this method as CID/ETnoD. The use of a multistage CID activation (CID) and ETnoD protocol has been applied to several intact proteins to obtain multiple sequence identifications.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11228978 | PMC |
| http://dx.doi.org/10.1021/jasms.4c00108 | DOI Listing |
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