Physicochemical mechanism of BSA, Hb, and dsDNA biomacromolecules with aq-NaCMC at 298.15–310.15 K interfaced with UV–vis fluorescence circular dichroism spectroscopy and in-silico for interacting activities

The 0.2–0.8mg% @ 0.2 mg% bovine serum albumin (BSA 66), hemoglobin (Hb 64.5), and double stranded deoxyribonucleic acid (dsDNA 130 kDa) with water and 0.25, 0.50, and 1.00 g% aqueous carboxymethyl cellulose sodium salt (NaCMC) thermodynamically, kinetically, and tentropically stable homogeneous solutions via resonating energy transfer were designed. Density (ρ), viscosity (η), surface tension (γ), friccohesity (σ), Gibbs free energy (ΔGb), chemical potential (μ), frictional volume (ϕ), apparent molar volume (V2), hydrodynamic radius (Rh), and isentropic compressibility (ksϕ) at 298.15, 304.15, and 310.15 K were studied. UV–Vis spectrophotometry, fluorescence spectroscopy, circular dichroism (CD), MALDI TOF, and in-silico study via reorientational activities have elucidated structural recognition. The ρ, η, γ, σ, ΔGb, μ, V2, ϕ, Rh, and ksϕ physicochemical properties (PCPs) have studied the interacting activities of salt bridges (peptide bonds) of proteins and base pairs (adenine, thymine, cytosine, guanine) of dsDNA on developing nanohydration sphere (NHS) with water and 0.25, 0.50, and 1.00 g% aq-NaCMC. Regression constants of PCPs have elaborated the interacting mechanism of internal linkages of BSA, Hb, and dsDNA for solubilizing them without unfolding assisted by glycosidic bonds of glucopyranose units of NaCMC. Magnitudes of regression constants analyse the inner salt bridges, electrostatic dipoles, and hydrogen bonds (HB) to interact with H2O dipoles and NaCMC affecting solubilization of biomolecules (biomols) in areas of biochemical, biophysical, bioengineering, tissue, and genetic engineering. PCPs, UV–Vis, fluorescence, CD, and in-silico study analyse their structurally interacting abilities with NaCMC via respective NHS to be extended to pharmaceutical and cosmetic processes by minimizing quantum energy barrier (QEB) as Newtonian behaviour of structural sensors.