Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins

dc.contributor.authorKumar, Rajesh
dc.contributor.authorKumar, Rajesh
dc.contributor.authorSharma, Deepak
dc.contributor.authorGarg, Mansi
dc.contributor.authorKumar, Vinay
dc.contributor.authorAgarwal, Mukesh Chand
dc.date.accessioned2019-03-22T07:47:12Z
dc.date.accessioned2024-08-13T11:02:31Z
dc.date.available2019-03-22T07:47:12Z
dc.date.available2024-08-13T11:02:31Z
dc.date.issued2018
dc.description.abstractStructural 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.citationKumar R., Kumar R., Sharma D. et.al. (2018) Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteinsen_US
dc.identifier.doi10.1016/j.bbapap.2018.08.012
dc.identifier.issn15709639
dc.identifier.urihttps://kr.cup.edu.in/handle/32116/2035
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S157096391830147X
dc.language.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.subjectCold denaturationen_US
dc.subjectCrowding agentsen_US
dc.subjectEnthalpy-entropy ploten_US
dc.subjectMolten-globule stateen_US
dc.subjectThermal stabilityen_US
dc.titleMacromolecular crowding-induced molten globule states of the alkali pH-denatured proteinsen_US
dc.title.journalBiochimica et Biophysica Acta - Proteins and Proteomics
dc.typeArticleen_US

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