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from the pro-tein-comes-from-amateur-tein-that-has-had-lots-of-practice dept.
New Protein Sequencing Method Could Transform Biological Research
A team of researchers at The University of Texas at Austin has demonstrated a new way to sequence proteins that is much more sensitive than existing technology, identifying individual protein molecules rather than requiring millions of molecules at a time. The advance could have a major impact in biomedical research, making it easier to reveal new biomarkers for the diagnosis of cancer and other diseases, as well as enhance our understanding of how healthy cells function.
[...] The current laboratory standard for sequencing proteins, using a tool called mass spectrometry, is not sensitive for many applications — it can detect a protein only if there are about a million copies of it. It also has a "low throughput," meaning it can detect only a few thousand distinct protein types in a single sample.
With this new method, called single molecule fluorosequencing, researchers can now sequence millions of individual protein molecules simultaneously in a single sample. Marcotte believes with future refinements the number of molecules that could be detected in a sample could reach into the billions. With higher throughput and much greater sensitivity than existing technology, the tool should allow for greater detection of biomarkers of disease and would also make it possible to study things such as cancer in a whole new way. For example, researchers could look, cell-by-cell, to understand how a tumor evolves from a small mass of identical cells to a soup of genetically divergent cells, each with its own strengths and weaknesses. Such insights could inspire novel ways to attack cancer.
Highly parallel single-molecule identification of proteins in zeptomole-scale mixtures (DOI: 10.1038/nbt.4278) (DX)
(Score: 3, Interesting) by ikanreed on Tuesday October 23 2018, @03:54PM
First off, a quick thank you to the op for the hint hint wink wink of including the DOI alongside the link to the abstract. You know it's for sci-hub, I know it's for sci-hub, but the cops can't prove it.
Second, it looks like all their sampled proteins in the body of the paper are very short and without folds, like Insulin-A2 and RK†TTRK†M. The whole amino-radical recursion thing they do might fall apart on a longer, more complex protein. The NH2 might hit a juncture and the process of iterating to the next amino acid might activate entirely incorrectly.
Third, the uses for this have to be pretty specific considering the process expense and complexity compared to genetic sequencing. If you're trying to analyze expression levels, RNA sequencing is really good and afforableish now. Which leaves this tool in the space of analyzing cases of mystery proteins with unknown genes, and testing hypotheses about proteins that are expressed differently than their respective genome suggests(e.g. prions).