Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins
dc.contributor.author | Kumar, Rajesh | |
dc.contributor.author | Kumar, Rajesh | |
dc.contributor.author | Sharma, Deepak | |
dc.contributor.author | Garg, Mansi | |
dc.contributor.author | Kumar, Vinay | |
dc.contributor.author | Agarwal, Mukesh Chand | |
dc.date.accessioned | 2019-03-22T07:47:12Z | |
dc.date.accessioned | 2024-08-13T11:02:31Z | |
dc.date.available | 2019-03-22T07:47:12Z | |
dc.date.available | 2024-08-13T11:02:31Z | |
dc.date.issued | 2018 | |
dc.description.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 B -states). These results further revealed that the C B -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. - 2018 Elsevier B.V. | en_US |
dc.identifier.citation | Kumar R., Kumar R., Sharma D. et.al. (2018) Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins | en_US |
dc.identifier.doi | 10.1016/j.bbapap.2018.08.012 | |
dc.identifier.issn | 15709639 | |
dc.identifier.uri | https://kr.cup.edu.in/handle/32116/2035 | |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S157096391830147X | |
dc.language.iso | en_US | en_US |
dc.publisher | Elsevier B.V. | en_US |
dc.subject | Cold denaturation | en_US |
dc.subject | Crowding agents | en_US |
dc.subject | Enthalpy-entropy plot | en_US |
dc.subject | Molten-globule state | en_US |
dc.subject | Thermal stability | en_US |
dc.title | Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins | en_US |
dc.title.journal | Biochimica et Biophysica Acta - Proteins and Proteomics | |
dc.type | Article | en_US |
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