QCAL—a Novel Standard for Assessing Instrument Conditions for Proteome Analysis

If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capabl...

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Published inJournal of the American Society for Mass Spectrometry Vol. 19; no. 9; pp. 1275 - 1280
Main Authors Eyers, Claire E., Simpson, Deborah M., Wong, Stephen C.C., Beynon, Robert J., Gaskell, Simon J.
Format Journal Article
LanguageEnglish
Published New York Elsevier Inc 01.09.2008
Springer-Verlag
Elsevier Science
Springer Nature B.V
Subjects
Online AccessGet full text
ISSN1044-0305
1879-1123
DOI10.1016/j.jasms.2008.05.019

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Abstract If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli, provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics. QCAL1 is described as a novel tool for the assessment and optimization of instruments used in proteome analyses, providing a platform for standardization.
AbstractList If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli , provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics.
If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli, provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics. QCAL1 is described as a novel tool for the assessment and optimization of instruments used in proteome analyses, providing a platform for standardization.
If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli, provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics.
If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli, provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics.If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents for optimization and standardization of instrument performance. At present, there is no single protein or peptide standard set that is capable of assessing instrument performance for peptide separation and analysis in this manner. To create such a standard, we have used the recently described QconCAT methodology to generate an artificial protein, QCAL. This protein, a concatenation of tryptic peptides that is expressed in E. coli, provides a stoichiometrically controlled mixture of peptides that are amenable to analysis by all commonly used instrumentation platforms for proteomics.
Author Eyers, Claire E.
Wong, Stephen C.C.
Simpson, Deborah M.
Gaskell, Simon J.
Beynon, Robert J.
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  givenname: Claire E.
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  fullname: Wong, Stephen C.C.
  organization: Michael Barber Centre for Mass Spectrometry, Manchester Interdisciplinary Biocentre, School of Chemistry, University of Manchester, Manchester, United Kingdom
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  organization: Michael Barber Centre for Mass Spectrometry, Manchester Interdisciplinary Biocentre, School of Chemistry, University of Manchester, Manchester, United Kingdom
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Issue 9
Keywords Tryptic Peptide
Instrument Resolution
Artificial Protein
Peptide
Homoarginine
Tandem mass spectrometry
Fourier transformation
Peptides
Coupled method
HPLC chromatography
Proteome
Matrix assisted laser desorption ionization
Ion cyclotron resonance spectrometry
Electrospray
Optimization
Protein
Operating conditions
Reversed phase chromatography
Analysis method
Synthetic product
Peptide fragment
Time of flight method
Polypeptide
Proteomics
Mass spectrometry
Language English
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Snippet If proteome datasets are to be collated, shared, and merged for higher level proteome analyses, there is a need for generally accepted strategies and reagents...
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SubjectTerms Amino Acid Sequence
Analytical Chemistry
Analytical, structural and metabolic biochemistry
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bioinformatics
Biological and medical sciences
Biotechnology
Chemistry
Chemistry and Materials Science
Chromatography, High Pressure Liquid
E coli
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Mass spectrometry
Molecular Sequence Data
Nanotechnology
Organic Chemistry
Peptides
Peptides - analysis
Proteins
Proteomics
Proteomics - methods
Proteomics - standards
Reagents
Reference Standards
Short Communication
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Spectroscopy, Fourier Transform Infrared - methods
Standardization
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Title QCAL—a Novel Standard for Assessing Instrument Conditions for Proteome Analysis
URI https://dx.doi.org/10.1016/j.jasms.2008.05.019
https://link.springer.com/article/10.1016/j.jasms.2008.05.019
https://www.ncbi.nlm.nih.gov/pubmed/18599307
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Volume 19
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