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CCMB Scientists discover how protein flexibility enables binding with multiple partners

Hyderabad, May 7 (UNI) In a groundbreaking discovery, scientists at the Centre for Cellular and Molecular Biology (CCMB) have revealed that the function of proteins is not solely determined by their fixed three-dimensional structures.
Instead, their ability to dynamically change shape plays a critical role in enabling them to interact with multiple molecular partners.

According to a study published in the Journal of the American Chemical Society, researchers found that two plant proteins with identical structures display different substrate specificities because one is significantly more flexible.

This flexibility allows the protein to bind with a broader range of RNA molecules by transiently rearranging itself to match the shape of its partners, without compromising structural stability. This capability is essential for complex gene regulation.

Using a powerful technique called nuclear magnetic resonance (NMR) spectroscopy, along with advanced computational modelling, the researchers detected minute populations—just 1 per cent—of protein molecules that transiently switch into different structural forms. These rare conformational changes were found to be crucial in recognising diverse RNA targets and help explain how plants achieve intricate gene regulation using a limited number of proteins.

“What we have shown is that a protein’s ability to change shape, even slightly, can be just as important as its structure,” said Dr. Mandar V. Deshmukh, lead author of the study. “By capturing these fleeting dynamic states, we’ve demonstrated that structural flexibility during molecular interactions provides a functional advantage in complex cellular environments. This insight could reshape approaches to drug design and agricultural biotechnology.”

The study further highlights how subtle differences in protein sequences—particularly in regions outside of the active site—can drastically affect their function. This underlines the importance of examining both structural and dynamic properties of proteins, especially those that serve as targets for therapeutic drugs.

“Our results reveal nature’s originality in granting versatility to a few proteins through minimal design tweaks,” said Debadutta Patra and Jaydeep Paul, joint first authors of the paper.

The findings also offer a potential explanation for how plants fine-tune RNA processing with a limited set of proteins, especially in the absence of adaptive immune systems. By leveraging these insights, researchers hope to develop more efficient multitasking proteins for use in medicine, agriculture, and biotechnology.
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