Latest news with #MandarVDeshmukh
Time of India
09-05-2025
- Science
- Time of India
CSIR-CCMB scientists uncover how protein flexibility enables multitasking in plants
1 2 Hyderabad: New research from Council of Scientific & Industrial Research (CSIR) – Centre for Cellular and Molecular Biology (CCMB) has revealed that proteins do not always rely on a fixed three-dimensional shape to perform their functions. Instead, their structures can be flexible, enabling them to carry out multiple roles. This insight reshapes our understanding of protein dynamics in biological study provides a plausible explanation for how plants fine-tune RNA processing without expanding their protein repertoire, particularly in the absence of adaptive immunity. These findings could pave the way for advances in medicine, agriculture, and biotechnology by assisting scientists in designing proteins capable of multitasking more to a study published in the Journal of the American Chemical Society, two structurally identical plant proteins exhibit varied substrate specificity due to differences in flexibility. Operation Sindoor PM Modi meets NSA, chiefs of armed forces amid spike in tensions with Pak India's air defence systems shoot down Pak drones in J&K, Punjab & Rajasthan Several airports in India to be closed till May 15 - check list One of the proteins, being more flexible, can bind to a broader range of substrate RNA molecules by dynamically rearranging itself to accommodate the shapes of its molecular partners without compromising stability, which is crucial for gene artwork illustrates the various structures the RNA-binding protein (shown as the largest structure in the left corner) can interact with. Using a powerful technique called nuclear magnetic resonance (NMR) spectroscopy, combined with sophisticated computational methods, scientists identified tiny populations, just 1%, of protein structures that temporarily switch into different shapes. These rare transitions are essential for recognising diverse RNA forms and help explain how plants manage complex gene regulation using fewer Mandar V Deshmukh, lead author of the study, said, "What we have shown is that a protein's ability to change shape, even slightly, can be just as important as its structure." He added, "By capturing the fleeting, dynamic states of these proteins, we've demonstrated that their capacity to transiently rearrange their structure by flexing and adjusting during interaction gives them a functional advantage in complex cellular environments. This enables organisms to regulate genes efficiently under varying conditions. It could transform how we think about developing new medicines or enhancing plant traits."The study also highlights how subtle changes in a protein's sequence, within just a few non-active site amino acid residues, can lead to significant functional differences. This underscores the importance of studying both structure and dynamics, particularly for proteins that are potential drug targets."Our results reveal nature's originality in designing a unique approach to grant promiscuity to a few proteins," said Debadutta Patra and Jaydeep Paul, joint first authors of the study.
Hans India
09-05-2025
- Health
- Hans India
CCMB researchers discover key role of protein agility in binding to different molecular partners
Hyderabad: Scientists at the Centre for Cellular and Molecular Biology (CCMB) have recently made a significant discovery: proteins can perform multiple functions by temporarily changing their shape, not only based on their fixed three-dimensional structure but also through their flexibility. The study, published in the Journal of the American Chemical Society, reveals that two structurally identical plant proteins exhibit different substrate specificities, allowing them to recognise distinct substrates. The key difference is that one of the proteins is more flexible than the other. This enhanced flexibility enables it to bind to various types of RNA molecules, as the protein can dynamically rearrange its structure to align with the shape of its partner molecules. This property is crucial for gene regulation. Using nuclear magnetic resonance (NMR) spectroscopy and advanced computational methods, researchers identified transient protein structures that constitute only 1 per cent of the total protein. These structures, which briefly change shape, play a vital role in recognising different RNA forms. 'We demonstrated that a protein's ability to change shape slightly is just as important as its stable structure,' said lead author Dr Mandar V Deshmukh. Through these transient dynamic states, proteins can function efficiently in the complex conditions of the cellular environment, helping organisms to regulate their genes properly under changing circumstances. This discovery could lead to revolutionary advancements in drug design and the improvement of plant traits in the future.' The study also revealed that changes in a few amino acids in non-active site residues of a protein can result in significant functional differences. This underscores the importance of comprehensively studying both structure and dynamics, particularly in the development of drug target proteins. 'The ability of some proteins to perform multiple functions, known as functional promiscuity, reflects one of Nature's originalities,' noted Debadutta Patra and Jaydeep Paul, joint first authors of the study. The research highlights how plants precisely control RNA processing using fewer proteins and without the need for an adaptive immune system. Scientists believe this study could pave the way for new discoveries in medicine, agriculture, and biotechnology.
