TY  - JOUR
N1  - Copyright of this article belongs to Elsevier Science.
ID  - open2144
UR  - https://www.sciencedirect.com/science/article/pii/S157096391830147X?via%3Dihub
IS  - 11
A1  - Kumar, Rajesh
A1  - Kumar, Rajesh
A1  - Sharma, Deepak
A1  - Garg, Mansi
A1  - Kumar, Vinay
A1  - Agarwal, Mukesh Chand
Y1  - 2018/11/11/
N2  - 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.
PB  - Elsevier Science
JF  - Biochimica et biophysica acta. Proteins and proteomics
VL  - 1866
KW  - Cold denaturation; Crowding agents; Enthalpy-entropy plot; Molten-globule state; Thermal stability
SN  - 1878-1454
TI  - Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.
SP  - 1102
EP  - 1114
ER  -