Published On : 2019-06-03
A collaborative research by the University of Massachusetts (UMass) Amherst and the University of Illinois Urbana-Champaign has paved the way for scientists to predict as well as understand behavior of disordered polymers and proteins. Furthermore, the findings of the research will help in reading patterns of long chains of molecules. In addition, the study is said to help in the development of new materials from synthetic polymers. The theory behind the discovery was prepared by the laboratory of University of Illinois at Urbana-Champaign’s Assistant Professor of Chemical and Biomolecular Engineering, Charles Sing. On the other hand, the laboratory of UMass Amherst’s Assistant Professor of Chemical Engineering Sarah Perry performed experiments to verify Sing’s theory.
“We are taking inspiration from a biological system, and this I think is the exciting thing about this work. A protein’s typical image shows it folds into a highly precise structure. However, this system is based around proteins that are intrinsically disordered,” said Sing.
The research builds on earlier findings of Sing and Perry in 2017
The research study was published in ACS Central Science through a paper carrying the title “Designing Electrostatic Interactions via Polyelectrolyte Monomer Sequence.” The paper builds on Sing and Perry’s previous findings in 2017. The collaborators began their research by understanding the physics responsible for charged monomers’ precise sequence along the chain. They also took efforts to understand how this physics affects the ability of polymers for creating complex coacervates or self-assembling liquid materials.
“Our previous paper explained that these sequences do matter. This paper explains why they do matter. The first explained that in complex coacervation different properties are given by different sequences. Now, what we are able to do is employ a theory to predict actually why they are behaving in this manner,” said Sing.
Sing also explained that most synthetic polymers do not interact with binding partners that are very specific, unlike structured proteins. In fact, synthetic polymers are fuzzier, and they react with a broad scope of molecules in their surroundings. Despite of this, the researchers observed that the monomers’ precise sequence along a protein really makes a difference.
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