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Structural integrity and functional properties of protein are governed by arrangement and side-chain nature of every amino acid constituting it. Substitution mutations have been observed in many proteins which are very important for cellular functions. The current study aims to understand the molecular basis of protein stability, and solubility using SOD1 enzyme where multiple point mutations are have been reported. Around 51 point mutations reported in the SOD1 enzyme were retrieved from ALSoD and HuVarBase databases. The mutations were grouped based on the properties of amino acid residue involved. The impact of mutations on SOD1 function was predicted using PROVEAN and changes in the structural stability induced by point mutation was evaluated based on free energy change using Foldx. Influence of mutation on SOD1 solubility was studied using CamSol Intrinsic web server. The mutations resulting from the substitution of polar and charged residues were found to influence functionally important state, free energy value and solvent interaction of the protein. This study hypothesizes that the physicochemical properties of every amino acid residue constituting protein, influence the stability and solubility of the protein. The future prospect includes establishing a correlation between these two properties to identify factors driving protein aggregation upon point mutation.

Effect of Point Mutations in SOD1 Enzyme Stability and Solubility: A Study Using Computational Approach