%A Rajesh Kumar
%A Rajesh Kumar
%A Deepak Sharma
%A Mansi Garg
%A Vinay Kumar
%A Mukesh Chand Agarwal
%O Copyright of this article belongs to Elsevier Science.
%J Biochimica et biophysica acta. Proteins and proteomics
%T Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.
%X Structural and molecular properties extracted from circular dichroism (CD), tryptophan fluorescence and 1-anilino-8-napthalene sulfonate (ANS) binding experiments suggest that the high concentration of synthetic crowding agents (dextran 40, dextran 70 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 (C-states). These results further revealed that the C-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 ?-loop that control CO association to alkaline Ferrocyt c.
%N 11
%K Cold denaturation; Crowding agents; Enthalpy-entropy plot; Molten-globule state; Thermal stability
%P 1102-1114
%V 1866
%D 2018
%I Elsevier Science
%L open2144