Citraconylation - a simple method for high protein sequence coverage in MALDI-TOF mass spectrometry

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008939" target="_blank" >RIV/60461373:22330/03:00008939 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Citraconylation - a simple method for high protein sequence coverage in MALDI-TOF mass spectrometry
Original language description
Lysine ?-amino group reacts with citraconic anhydride forming a derivative which is stable on terms for trypsin cleavage. This modification changes the spectrum of peptides formed by the trypsin action; as the number of trypsin-sensitive sites is reduced, the peptides with higher molecular mass can survive in the digest. The various studies of proteins by MALDI-TOF mass spectrometry are often complicated by the low sequence coverage of the peptide chain. This paper demonstrates that the modification ofproteins by citraconylation before trypsin cleavage represents a simple experimental technique which allows a significant increase of sequence coverage in MALDI-TOF mass spectrometry. This improvement is caused both by change of trypsin fragmentation pattern and by disturbance of the protein's native tertiary structure.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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