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Curr Opin Chem Biol. 2015 Feb;24:11-7. doi: 10.1016/j.cbpa.2014.10.017. Epub 2014 Nov 8.

Proteome sequencing goes deep.

Author information

1
Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, United States; Genome Center of Wisconsin, University of Wisconsin-Madison, 425 Henry Mall, Madison, WI 53706, United States.
2
Genome Center of Wisconsin, University of Wisconsin-Madison, 425 Henry Mall, Madison, WI 53706, United States.
3
Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, United States; Genome Center of Wisconsin, University of Wisconsin-Madison, 425 Henry Mall, Madison, WI 53706, United States; Department of Biomolecular Chemistry, University of Wisconsin-Madison, 420 Henry Mall, Madison, WI 53706, United States. Electronic address: jcoon@chem.wisc.edu.

Abstract

Advances in mass spectrometry (MS) have transformed the scope and impact of protein characterization efforts. Identifying hundreds of proteins from rather simple biological matrices, such as yeast, was a daunting task just a few decades ago. Now, expression of more than half of the estimated ∼20,000 human protein coding genes can be confirmed in record time and from minute sample quantities. Access to proteomic information at such unprecedented depths has been fueled by strides in every stage of the shotgun proteomics workflow-from sample processing to data analysis-and promises to revolutionize our understanding of the causes and consequences of proteome variation.

PMID:
25461719
PMCID:
PMC4308434
DOI:
10.1016/j.cbpa.2014.10.017
[Indexed for MEDLINE]
Free PMC Article

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