Factors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitro
dc.contributor.author | Kumar, Rajesh | |
dc.contributor.author | Sharma, Deepak | |
dc.contributor.author | Kumar, Vinay | |
dc.contributor.author | Kumar, Rajesh | |
dc.date.accessioned | 2019-03-26T09:07:54Z | |
dc.date.accessioned | 2024-08-13T11:02:32Z | |
dc.date.available | 2019-03-26T09:07:54Z | |
dc.date.available | 2024-08-13T11:02:32Z | |
dc.date.issued | 2018 | |
dc.description.abstract | The 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.citation | Kumar, 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.doi | 10.1016/j.abb.2018.07.018 | |
dc.identifier.issn | 0003-9861 | |
dc.identifier.uri | https://kr.cup.edu.in/handle/32116/2267 | |
dc.identifier.url | https://www.sciencedirect.com/science/article/abs/pii/S0003986118302133 | |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.subject | Crowding agents | en_US |
dc.subject | Constrained dynamics | en_US |
dc.subject | Thermodynamic stability | en_US |
dc.subject | Counteracting effect | en_US |
dc.subject | Excluded volume effect | en_US |
dc.title | Factors Defining the Effects of macromolecularcrowding on dynamics and thermodynamics stability of heme proteins in-vitro | en_US |
dc.title.journal | Archives of biochemistry and biophysics | en_US |
dc.type | Article | en_US |
dc.type.accesstype | Closed Access | en_US |