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

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Studium konformace bílkovin pomocí hmotnostní spektrometrie na principu MALDI-TOF (Matrix Assisted Laser Desorption Ionisation - Time Of Flight)</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochemical and Biophysical Research Communications

ISSN

0006-291X

e-ISSN

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Svazek periodika

61

Číslo periodika v rámci svazku

305

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

3

Strana od-do

1091-1093

Kód UT WoS článku

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EID výsledku v databázi Scopus

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