Kumar, RajeshKumar, RajeshSharma, DeepakGarg, MansiKumar, VinayAgarwal, Mukesh Chand2019-03-262024-08-132019-03-262024-08-132018Kumar, Rajesh., Kumar, Rajesh., Sharma, Deepak and et. al. (2018) Macromolecular crowding on Dynamics and Thermodynamic Stability of Heme Proteins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Vol. 1866 (11), PP. https://doi.org/10.1016/j.bbapap.2018.08.0121570-963910.1016/j.bbapap.2018.08.012https://kr.cup.edu.in/handle/32116/2266Structural and molecular properties extracted from circular dichroism (CD), tryptophanfluorescence and 1-anilino-8-napthalene sulfonate (ANS) binding experiments suggest that the high concentration of synthetic crowding agents (dextran 40, dextran70 and ficoll 70) stabilizes and refolds the base-denatured ferricytochrome c (Ferricyt c) and lysozyme (Lyz) at pH 12.9 (±0.1) to molten globule (MG) states (CB-states). These results further revealed that the CB-states resemble the generic properties of MG-states. Thermodynamic analysis of thermal denaturation curves of base-denatured Ferricyt c and Lyz at pH 12.9 (±0.1) under variable concentrations of crowding agents (dextran 40, dextran 70 and ficoll 70) revealed that the crowder presence increases the thermal stability of base-denatured proteins and also prevents the cold denaturation of Ferricyt c. The results further showed that the nature, size and shape of crowder influence the crowding-mediated increase in secondary structure stabilization and thermal stability of base-denatured Ferricyt c and Lyz. Analysis of kinetic and thermodynamic parameters measured for CO association reaction of alkaline ferrocytochrome c (Ferrocyt c) at pH 12.9 (±0.1) under variable concentrations of crowding agents (dextran 40, dextran 70 and ficoll 70) revealed that the crowder presence reduces the level of structural fluctuation of M80-containing Ω-loop that control CO association to alkaline Ferrocyt c.enMolten-globule stateCrowding agentsThermal stabilityCold denaturationEnthalpy-entropy plotArticlehttps://www.sciencedirect.com/science/article/pii/S157096391830147X?via%3Dihub