Original story from Rice University (TX, USA). A simple way to study a common but overlooked posttranslational modification has been developed, unlocking new insights into how proteins function Amino acids are like Lego blocks; they can be linked together to form complex structures called proteins. Unlike Legos, however, there are only 20 different types of amino acids available to build a protein. Proteins depend on posttranslational modifications, or chemical changes to an amino acid that happen after the protein is built, to achieve many of their forms and functions by expanding how an amino acid can behave. Rice University (TX, USA) chemistry professor Zachary Ball recently published a paper describing a new way to target a common but understudied posttranslational modification called pyroglutamate. Pyroglutamate occurs when a chemical reaction makes a ring at an amino acid called glutamate, expelling a molecule of water in the process. This alteration is difficult to study because it doesn’t leave a big change in the protein, explaining why so little is known about this ubiquitous modification. Illuminating the link between amyloid beta and tau in Alzheimer’s disease New research suggests Alzheimer’s arises not simply from plaques forming in the brain, but from one protein interfering with the normal job of another. “We don’t know a lot about pyroglutamate beyond that we see it frequently,” shared Ball, the corresponding author on this paper. “With this new technique, we can now start to ask questions about its distribution patterns and the roles it may play in…
