Comprehensive Characterization of dl-Valine: Molecular Structure, Vibrational Analysis, Biological Implication and Molecular Dynamics Simulation

dl-Valine (dl-Val), a pivotal amino acid essential for protein synthesis, exhibits a complex molecular structure. Validation of computational methods against experimental measurements of parameters such as bond lengths and angles was done carefully. The computational vibrational spectra analysis demonstrates accurate predictions of C–H, C–N, –NH 2 , C[Formula: see text]O, O–H and C–C vibrations, aligned closely with experimental IR data. Furthermore, MEP mapping and ELF analysis elucidate dl-Val’s charge distribution and electron density, offering insights into its reactivity and intermolecular interactions. Non-covalent interactions within the titled molecule are highlighted by the RDG visualization. The Fukui function study provided empirical data on the molecule’s nucleophilic and electrophilic sites, crucial for predicting its interactions with other molecules. The electronic structure was assessed through FMO theory, highlighting its strength and chemical properties. UV–Vis spectroscopy was utilized to study its absorption spectra in different solvents, revealing consistent optical behavior across phases. Thermodynamic parameters elucidated its stability and energetic properties over a range of temperatures. Hirshfeld surface analysis presented a detailed view of its crystal interactions, emphasizing H-bonding motifs. Molecular docking studies with various protein targets underscored its potential biological activity, supported by favorable drug-likeness profiles derived from ADME calculations. MDS was performed to analyze its atomic charges, revealing insights into molecular polarizability and reactivity. This integrated approach provides a comprehensive understanding of the desired molecule’s potential applications in pharmaceutical and biochemical research.