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PAS‐cal: A repetitive peptide sequence calibration standard for MALDI mass spectrometry
Author(s) -
Maier Stefan K.,
Bashkueva Ksenia,
Rösli Christoph,
Skerra Arne,
Kuster Bernhard
Publication year - 2014
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201400199
Subject(s) - mass spectrometry , mass spectrum , peptide , chemistry , chromatography , peptide mass fingerprinting , tandem mass spectrometry , matrix assisted laser desorption/ionization , analytical chemistry (journal) , tandem mass tag , proteomics , protein mass spectrometry , bottom up proteomics , peptide sequence , calibration , quantitative proteomics , desorption , physics , biochemistry , organic chemistry , adsorption , quantum mechanics , gene
Mass spectrometers equipped with matrix‐assisted laser desorption/ionization (MALDI‐MS) require frequent multipoint calibration to obtain good mass accuracy over a wide mass range and across large numbers of samples. In this study, we introduce a new synthetic peptide mass calibration standard termed PAS‐cal tailored for MALDI‐MS based bottom‐up proteomics. This standard consists of 30 peptides between 8 and 37 amino acids long and each constructed to contain repetitive sequences of Pro, Ala and Ser as well as one C‐terminal arginine residue. MALDI spectra thus cover a mass range between 750 and 3200 m/z in MS mode and between 100 and 3200 m/z in MS/MS mode. Our results show that multipoint calibration of MS spectra using PAS‐cal peptides compares well to current commercial reagents for protein identification by PMF. Calibration of tandem mass spectra from LC‐MALDI experiments using the longest peptide, PAS‐cal37, resulted in smaller fragment ion mass errors, more matching fragment ions and more protein and peptide identifications compared to commercial standards, making the PAS‐cal standard generically useful for bottom‐up proteomics.