Protein complexes are important for the majority of vital processes in the cell and human body, such as producing energy, copying DNA and regulating the immune system.
Composed of groups of connected protein chains called subunits, the complexes are also good targets for medicines that treat diseases.
But studying them in their native, natural physiological state, while preserving their 3-D protein folds, has proved challenging.
Traditional mass spectrometry methods and structural biology techniques may require breaking protein chains into pieces or turning protein parts into crystals.
These approaches not only disrupt the structure of the assembled protein molecules but involve using substantial amounts of samples and waiting weeks for results.
Now researchers at Northeastern University have developed a novel method of preserving the structure of protein complexes and their interactions under near-native conditions while analyzing them in 30 minutes or less, using small sample amounts.
Associate research scientist Anne-Lise Marie and associate professor of chemistry and chemical biology Alexander R. Ivanov say their research, published in the Advanced Science journal, could eventually expedite drug development for pathologies such as Alzheimer’s and Parkinson’s disease.
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Photo by Alyssa Stone/Northeastern University
