A major puzzle of biology is that while the human genome contains roughly 20,000 genes, many comparatively primitive organisms — including the universally-studied worm C. elegans — have almost the same number of genes.
If not genes alone, what accounts for that quantum leap in complexity between the two species?
One answer may lie in the field of proteomics, which focuses on identifying and defining the protein building blocks that make up an individual cell. Rather than one gene coding for one protein with one purpose, human genes act like powerful compressed files, where a single gene can code for hundreds of distinct proteins that each perform precise functions in the body.
As many as 95% of human genes have this capability, known as alternative splicing.
A new study released in the journal Nature Biotechnology outlines a meta-scale approach to quantifying the human proteome and the massive number of protein variants produced by the human body. Proteomics is a cornerstone of biology and a precursor to understanding how protein dysfunction contributes to disease.
Led by Joshua Coon, professor of biomolecular chemistry and investigator at the Morgridge Institute for Research, the research team developed a method called “deep proteome sequencing” that offers unprecedented characterization of the proteins that show up in standard proteomics experiments.
Written by Brian Mattmiller.