creators_name: Kumar, Rajesh
creators_name: Kumar, Rajesh
creators_name: Sharma, Deepak
creators_name: Garg, Mansi
creators_name: Kumar, Vinay
creators_name: Agarwal, Mukesh Chand
type: article
datestamp: 2019-03-19 09:45:41
lastmod: 2019-03-19 09:45:41
metadata_visibility: show
title: Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.
ispublished: pub
subjects: QR
keywords: Cold denaturation; Crowding agents; Enthalpy-entropy plot; Molten-globule state; Thermal stability
note: Copyright of this article belongs to Elsevier Science.
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 (±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 Ω-loop that control CO association to alkaline Ferrocyt c.
date: 2018-11-11
date_type: published
publication: Biochimica et biophysica acta. Proteins and proteomics
volume: 1866
number: 11
publisher: Elsevier Science
pagerange: 1102-1114
refereed: TRUE
issn: 1878-1454
official_url: https://www.sciencedirect.com/science/article/pii/S157096391830147X?via%3Dihub
citation:   Kumar, Rajesh and Kumar, Rajesh and Sharma, Deepak and Garg, Mansi and Kumar, Vinay and Agarwal, Mukesh Chand  (2018) Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins.  Biochimica et biophysica acta. Proteins and proteomics, 1866 (11).  pp. 1102-1114.  ISSN 1878-1454