Factors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitro

dc.contributor.authorKumar, Rajesh
dc.contributor.authorSharma, Deepak
dc.contributor.authorKumar, Vinay
dc.contributor.authorKumar, Rajesh
dc.date.accessioned2019-03-26T09:07:54Z
dc.date.accessioned2024-08-13T11:02:32Z
dc.date.available2019-03-26T09:07:54Z
dc.date.available2024-08-13T11:02:32Z
dc.date.issued2018
dc.description.abstractThe role of crowding agents on structure and activities of heme proteins has been established. Analysis of kinetic and thermodynamic parameters measured for CO-dissociation reaction of natively-folded carbonmonoxycytochrome c (NCO) and carbonmonoxymyoglobin (MbCO) at different [GdnHCl] or [Urea] in the presence of crowding agents (dextran 40, dextran 70 and ficoll 70) demonstrate that (i) at low denaturant concentrations, crowder presence enhances the denaturant-mediated restricted dynamics of NCO and MbCO, and (ii) at higher denaturant concentrations, large scale unfolding-fluctuations dominate the dynamics and inclusion of crowder counteracts the structural-fluctuations causing the unfolding of proteins. Thermodynamic analysis of thermal and urea-unfolding curves of cytochrome c (Cyt c) and myoglobin (Mb) measured at different [GdnHCl] in presence of crowding agents reveals that crowder presence counterbalances and strengthens the destabilizing action of GdnHCl on stability of Cyt c and Mb, respectively. This study further demonstrates that the size, shape and concentration of crowding agent modulate the effect of crowder on denaturant-mediated dynamics and thermodynamic stability of heme proteins.en_US
dc.identifier.citationKumar, Rajesh., Sharma, Deepak., Kumar, Vinay and et. al. (2018) Factors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitro. Archives of biochemistry and biophysics. Vol. 654 , PP. 146-162. https://doi.org/10.1016/j.abb.2018.07.018.en_US
dc.identifier.doi10.1016/j.abb.2018.07.018
dc.identifier.issn0003-9861
dc.identifier.urihttps://kr.cup.edu.in/handle/32116/2267
dc.identifier.urlhttps://www.sciencedirect.com/science/article/abs/pii/S0003986118302133
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectCrowding agentsen_US
dc.subjectConstrained dynamicsen_US
dc.subjectThermodynamic stabilityen_US
dc.subjectCounteracting effecten_US
dc.subjectExcluded volume effecten_US
dc.titleFactors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitroen_US
dc.title.journalArchives of biochemistry and biophysicsen_US
dc.typeArticleen_US
dc.type.accesstypeClosed Accessen_US

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