{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T12:56:01Z","timestamp":1762865761829,"version":"build-2065373602"},"reference-count":29,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2011,1,24]],"date-time":"2011-01-24T00:00:00Z","timestamp":1295827200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Mass Spectrom."],"published-print":{"date-parts":[[2011,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Ammodytoxins (Atxs) are presynaptically neurotoxic phospholipases present in <jats:italic>Vipera ammodytes ammodytes<\/jats:italic> snake venom. Atxs show a high sequence homology and contain 14 cysteines which form seven biologically relevant disulfide bridges\u2014connecting non\u2010neighboring cysteines. Formic acid cleavage was performed to confirm protein sequences by MALDI RTOF MS and resulted in 95.6% sequence coverage exhibiting only few formylations. Cysteine\u2010containing peptides showed adjacent signals 2 and\/or 4 Da lower (according to the number of cysteines present in the peptide) than the theoretical molecular weight indicating disulfide bridge rearrangement. Post\u2010source decay (PSD) and high\u2010energy collision\u2010induced dissociation (CID) at 20 keV experiments showed fragmentation pattern unique for the reduced, thiol group containing and the oxidized, disulfide bridge harboring peptides. Besides typical low\u2010energy fragment ions observed during PSD experiments (<jats:italic>a<\/jats:italic>\u2010, <jats:italic>b<\/jats:italic>\u2010, <jats:italic>y<\/jats:italic>\u2010type ions), additional high\u2010energy fragment ions (<jats:italic>c<\/jats:italic>\u2010, <jats:italic>x<\/jats:italic>\u2010, <jats:italic>w<\/jats:italic>\u2010, <jats:italic>d<\/jats:italic>\u2010type and internal fragments) of significant intensity were generated during fragmentation at 20 keV. In the case of charge directing N\u2010 and C\u2010termini, <jats:italic>x<\/jats:italic>\u2010 and <jats:italic>w<\/jats:italic>\u2010type ions were also observed during PSD. Good and up to complete sequence coverage was achieved for all studied peptides from Atxs in the case of high\u2010energy CID, whereas PSD lacked information particularly for larger peptides. Copyright \u00a9 2011 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/jms.1871","type":"journal-article","created":{"date-parts":[[2011,1,24]],"date-time":"2011-01-24T01:55:02Z","timestamp":1295834102000},"page":"153-162","source":"Crossref","is-referenced-by-count":9,"title":["Studying disulfide bond rearrangement by MALDI\u2010RTOF PSD and MALDI\u2010TOF\/RTOF high\u2010energy CID (20 keV) experiments of peptides derived from ammodytoxins"],"prefix":"10.1002","volume":"46","author":[{"given":"Marija","family":"Brgles","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tihana","family":"Kurtovi\u0107","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Beata","family":"Halassy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G\u00fcnter","family":"Allmaier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martina","family":"Marchetti\u2010Deschmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2011,1,24]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jasms.2004.12.017"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac010619z"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(83)91030-3"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jasms.2009.07.007"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr0704682"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr070502c"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr700596e"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200500304"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijms.2008.04.030"},{"key":"e_1_2_6_11_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac061493e"},{"key":"e_1_2_6_12_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi051024r"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2009.10.010"},{"key":"e_1_2_6_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/ar000063m"},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac9707693"},{"key":"e_1_2_6_16_2","doi-asserted-by":"publisher","DOI":"10.1002\/mas.10025"},{"key":"e_1_2_6_17_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00216-008-2258-7"},{"key":"e_1_2_6_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jasms.2007.03.003"},{"key":"e_1_2_6_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja981948k"},{"key":"e_1_2_6_20_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr070142t"},{"key":"e_1_2_6_21_2","doi-asserted-by":"publisher","DOI":"10.1002\/rcm.3388"},{"key":"e_1_2_6_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijms.2009.08.008"},{"key":"e_1_2_6_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jchromb.2008.12.060"},{"key":"e_1_2_6_24_2","doi-asserted-by":"publisher","DOI":"10.2174\/138620709787315436"},{"key":"e_1_2_6_25_2","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1385\/1-59259-169-8:499","volume-title":"Protein Protoc. 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