@article{open2144,
          volume = {1866},
          number = {11},
           month = {November},
          author = {Rajesh Kumar and Rajesh Kumar and Deepak Sharma and Mansi Garg and Vinay Kumar and Mukesh Chand Agarwal},
            note = {Copyright of this article belongs to Elsevier Science.},
           title = {Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.},
       publisher = {Elsevier Science},
            year = {2018},
         journal = {Biochimica et biophysica acta. Proteins and proteomics},
           pages = {1102--1114},
        keywords = {Cold denaturation; Crowding agents; Enthalpy-entropy plot; Molten-globule state; Thermal stability},
             url = {http://crdd.osdd.net/open/2144/},
        abstract = {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 ({$\pm$}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 ({$\pm$}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 ({$\pm$}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.}
}