Osmolytes are generally well-known for the stabilization of proteins. The stabilizing impact of glucose on the dynamics and structure of myoglobin was probed through molecular simulation' docking and spectroscopic procedures. Using thermal stability examinations, the thermodynamic folding properties, point of melting temp. (Tm), thermodynamic enthalpy change (ΔH°) and thermodynamic entropy change (ΔS°) were determined to find out the depiction of myoglobin folding. Glucose operated as an enhancer relative to myoglobin stabilization. The quenching static model was demonstrated by fluorescence spectroscopy. There was one binding site. According to the spectroscopy analysis, glucose was capable of protecting the native structural conformation of protein as well as preventing from protein unfolding. The fluorescence spectroscopy together with simulation through molecular docking method revealed that definitely hydrogen bonding plus van der Waals forces had major contributions to the stabilization of the myoglobin-glucose complex. Hence, the direct interactions contributed slightly to the stabilization impact whereas indirect interactions resulted from the hydration arise from a molecular mechanism primarily inducing the glucose stabilizing impacts. An elevation occurred in the Tm of the myoglobin-glucose complex because of the greater H-bond creation and limited surface hydrophobic activity. Our findings indicate that glucose was capable of protecting the native conformation of myoglobin, clearly describing that glucose stabilization is preferred to be omitted from myoglobin surface. This is because water is more inclined to provide desirable interacting with myoglobin functional groups as compared to glucose. Also, MD results confirmed that the structural changes of myoglobin is the effect of complex formation with glucose.Communicated by Ramaswamy H. Sarma.
Keywords: Myoglobin; docking; fluorescence; glucose; thermal stability.