Abstract

Molecular dynamics the study of the motions, interactions, and conformational changes of biomolecules over time is central to understanding the functional mechanisms of proteins, nucleic acids, and other biomolecules. Traditional methods that provide static snapshots of molecular structures are complemented by biophysical techniques that can probe the dynamic behavior of molecules in real time. This manuscript reviews several cutting-edge biophysical methods for studying molecular dynamics, including single-molecule fluorescence spectroscopy, atomic force microscopy (AFM), circular dichroism (CD) spectroscopy, and fluorescence resonance energy transfer (FRET). These techniques offer unique advantages for observing conformational changes, molecular interactions, and forcedependent events on timescales ranging from femtoseconds to seconds. We discuss the principles behind each method, their applications in molecular biology and drug discovery, and the integration of these techniques for a more comprehensive understanding of biomolecular dynamics.