• Dr. Amit Kumar
• Shelly Bhardwaj

Comprehending protein dynamics, especially segmental relaxation, is essential for clarifying protein function. This work examines the segmental relaxation dynamics of the chemotaxis protein CheY (PDB ID: 3CHY), which is crucial in bacterial chemotaxis and serves as a model for cellular signaling pertinent to cancer research. We use Nuclear Magnetic Resonance (NMR) spectroscopy, coarse-grained molecular dynamics (MD) simulations, and Normal Mode Analysis (NMA) to offer an extensive perspective on CheY's dynamics. NMR spectroscopy elucidates longitudinal relaxation rates (R1), transverse relaxation rates (R2), and Nuclear Overhauser Effect (NOE) values, underscoring local flexibility. Coarse-grained molecular dynamics simulations compute Root-Mean-Square Fluctuation (RMSF) values, reflecting the dynamic behavior of residues. NMA delineates collective motions, differentiating between global and localized movements. Our findings indicate uniform local environments and adaptability in CheY, accompanied by areas exhibiting increased dynamic activity. This comprehensive method provides significant insights into the structure-function link of CheY and protein dynamics, enhancing the understanding of cellular signaling networks and prospective therapeutic targets.

"Comprehensive Analysis of Protein Segmental Relaxation Dynamics in CheY", International Journal of Emerging Technologies and Innovative Research (www.jetir.org), ISSN:2349-5162, Vol.11, Issue 9, page no.c667-c674, September-2024, Available :http://www.jetir.org/papers/JETIR2409272.pdf

"Comprehensive Analysis of Protein Segmental Relaxation Dynamics in CheY", International Journal of Emerging Technologies and Innovative Research (www.jetir.org | UGC and issn Approved), ISSN:2349-5162, Vol.11, Issue 9, page no. ppc667-c674, September-2024, Available at : http://www.jetir.org/papers/JETIR2409272.pdf