Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae
Several approaches have been described to identify proteins from MALDI MS/MS mass spectra. The sequence of tryptic peptides is determined by database searching or by de novo sequencing. Different algorithms are available to determine peptide sequence using mass spectra. False discovery of peptides i...
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crsagepubl:10.4137/pri.s3676 2023-05-15T14:11:30+02:00 Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae Kulkarni, Heramb M. Ramesh, V. Srinivas, R. Jagannadham, M.V. 2010 http://dx.doi.org/10.4137/pri.s3676 http://journals.sagepub.com/doi/pdf/10.4137/PRI.S3676 http://journals.sagepub.com/doi/full-xml/10.4137/PRI.S3676 en eng SAGE Publications http://journals.sagepub.com/page/policies/text-and-data-mining-license Proteomics Insights volume 3, page PRI.S3676 ISSN 1178-6418 1178-6418 Molecular Biology Biochemistry journal-article 2010 crsagepubl https://doi.org/10.4137/pri.s3676 2022-04-14T04:54:49Z Several approaches have been described to identify proteins from MALDI MS/MS mass spectra. The sequence of tryptic peptides is determined by database searching or by de novo sequencing. Different algorithms are available to determine peptide sequence using mass spectra. False discovery of peptides is an associated problem with it. A combination of chemical modifications followed by mass spectral analysis helps in overcoming this problem. Acetylating the tryptic peptides of β-galactosidase in methanol is found to increase the b-ion signal intensity in MALDI TOF mass spectrometry. The method of acetylation is extended to the tryptic peptides of the proteins of an Antarctic bacterium Pseudomonas syringae, whose genome sequence is not known. These proteins are identified by searching the available database of the Pseudomonas spp at NCBI using the MS/MS spectra. The sequences of the peptides are validated using the CID mass spectra of the acetylated tryptic peptides. Article in Journal/Newspaper Antarc* Antarctic SAGE Publications (via Crossref) Antarctic Proteomics Insights 3 PRI.S3676 |
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Open Polar |
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SAGE Publications (via Crossref) |
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English |
topic |
Molecular Biology Biochemistry |
spellingShingle |
Molecular Biology Biochemistry Kulkarni, Heramb M. Ramesh, V. Srinivas, R. Jagannadham, M.V. Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
topic_facet |
Molecular Biology Biochemistry |
description |
Several approaches have been described to identify proteins from MALDI MS/MS mass spectra. The sequence of tryptic peptides is determined by database searching or by de novo sequencing. Different algorithms are available to determine peptide sequence using mass spectra. False discovery of peptides is an associated problem with it. A combination of chemical modifications followed by mass spectral analysis helps in overcoming this problem. Acetylating the tryptic peptides of β-galactosidase in methanol is found to increase the b-ion signal intensity in MALDI TOF mass spectrometry. The method of acetylation is extended to the tryptic peptides of the proteins of an Antarctic bacterium Pseudomonas syringae, whose genome sequence is not known. These proteins are identified by searching the available database of the Pseudomonas spp at NCBI using the MS/MS spectra. The sequences of the peptides are validated using the CID mass spectra of the acetylated tryptic peptides. |
format |
Article in Journal/Newspaper |
author |
Kulkarni, Heramb M. Ramesh, V. Srinivas, R. Jagannadham, M.V. |
author_facet |
Kulkarni, Heramb M. Ramesh, V. Srinivas, R. Jagannadham, M.V. |
author_sort |
Kulkarni, Heramb M. |
title |
Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
title_short |
Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
title_full |
Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
title_fullStr |
Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
title_full_unstemmed |
Acetylating Tryptic Peptides Enhances b Ion Intensity in MALDI TOF/TOF: Implications in Peptide Sequencing and Identification of Proteins in an Antarctic Bacterium Pseudomonas Syringae |
title_sort |
acetylating tryptic peptides enhances b ion intensity in maldi tof/tof: implications in peptide sequencing and identification of proteins in an antarctic bacterium pseudomonas syringae |
publisher |
SAGE Publications |
publishDate |
2010 |
url |
http://dx.doi.org/10.4137/pri.s3676 http://journals.sagepub.com/doi/pdf/10.4137/PRI.S3676 http://journals.sagepub.com/doi/full-xml/10.4137/PRI.S3676 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Proteomics Insights volume 3, page PRI.S3676 ISSN 1178-6418 1178-6418 |
op_rights |
http://journals.sagepub.com/page/policies/text-and-data-mining-license |
op_doi |
https://doi.org/10.4137/pri.s3676 |
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Proteomics Insights |
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3 |
container_start_page |
PRI.S3676 |
_version_ |
1766283652000382976 |