Characterizing Collagen at the Double
Two-dimensional mass spectrometry (2DMS) can be twice as fast as conventional methods in proteomic analyses
James Strachan |
Conceived in the late 1980s, two-dimensional Fourier transform ion cyclotron resonance mass spectrometry (2D FT-ICR MS) correlates the mass-to-charge (m/z) ratio of fragment and precursor ions in a single spectrum, but was put on the backburner until recent advances in computer technology and algorithms gave researchers the necessary processing capability. And though some studies have taken advantage of the new tech to analyze a handful of smaller proteins and peptides, no group has analyzed a protein nearly as large as collagen – the subject of a new study by researchers at the University of Warwick (1). The researchers found that 2DMS could “uncoil collagen” two times faster than conventional methods.
“Collagen is a big protein, about 400 kDa, with many modified amino acids and crosslinks,” said Peter O'Connor, lead author of the study. “If we chop it into peptides using trypsin, and try to analyze the resulting mixture, there are thousands of peaks, and we can only assign a few dozen - the mixture is simply to complex.”
Read the full article now
Log in or register to read this article in full and gain access to The Analytical Scientist’s entire content archive. It’s FREE and always will be!
Or register now - it’s free and always will be!
You will benefit from:
- Unlimited access to ALL articles
- News, interviews & opinions from leading industry experts
- Receive print (and PDF) copies of The Analytical Scientist magazine
Or Login via Social Media
By clicking on any of the above social media links, you are agreeing to our Privacy Notice.