Native mass spectrometry reveals how lipids and proteins communicate at cell membranes
Charlotte Barker |
By visualizing molecular interactions in the cell membrane with a pioneering mass spectrometry (MS) method, researchers at Texas A&M University have shown how proteins are able to recruit a specific lipid microenvironment via allostery (1). A common feedback mechanism in biology, allostery is the regulation or modulation of a biological macromolecule through the binding of an effector ligand to a binding site other than the active site.
The Texas researchers have shown that this method of communication extends to lipids. When monitoring individual lipid binding with native ion mobility MS – a technique pioneered by group leader Arthur Laganowsky that preserves non-covalent interactions – the group noted that different lipid pairs exhibit various degrees of allosteric modulation.
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.