Studying disulfide bond rearrangement by MALDI-RTOF PSD and MALDI-TOF/RTOF high-energy CID (20 keV) experiments of peptides derived from ammodytoxins

Journal of Mass Spectrometry

Volumn 46, Issue 2, 2011, Pages 153-162

  Brgles, Marija ^a   Kurtović, Tihana ^a   Halassy, Beata ^a   Allmaier, Günter ^b   Marchetti Deschmann, Martina ^b  

^a INSTITUTE OF IMMUNOLOGY   (Croatia)

^b VIENNA UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

ammodytoxin; high energy CID; MALDI mass spectrometry; post source decay; vicinal disulfide bonds

Indexed keywords

AMMODYTOXIN; HIGH ENERGY; MALDI MASS SPECTROMETRY; POST-SOURCE DECAY; VICINAL DISULFIDE BONDS;

AMINO ACIDS; EXPERIMENTS; FORMIC ACID; IONS; MASS SPECTROMETRY; PEPTIDES;

HIGH ENERGY PHYSICS;

AMMODYTOXIN A; AMMODYTOXIN B; AMMODYTOXIN C; PHOSPHOLIPASE; SNAKE VENOM; UNCLASSIFIED DRUG;

ARTICLE; DISULFIDE BOND; ENERGY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; PRIORITY JOURNAL; SYNTHESIS;

AMINO ACID SEQUENCE; DISULFIDES; FORMIC ACIDS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; SEQUENCE ALIGNMENT; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; VIPER VENOMS;

VIPERA AMMODYTES AMMODYTES;

EID: 79951678397     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1871     Document Type: Article

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