Macromolecular crowding on Dynamics and Thermodynamic Stability of Heme 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.accessioned2019-03-26T09:07:54Z
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.abstractStructural and molecular properties extracted from circular dichroism (CD), tryptophanfluorescence and 1-anilino-8-napthalene sulfonate (ANS) binding experiments suggest that the high concentration of synthetic crowding agents (dextran 40, dextran70 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 (CB-states). These results further revealed that the CB-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.en_US
dc.identifier.citationKumar, Rajesh., Kumar, Rajesh., Sharma, Deepak and et. al. (2018) Macromolecular crowding on Dynamics and Thermodynamic Stability of Heme Proteins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Vol. 1866 (11), PP. https://doi.org/10.1016/j.bbapap.2018.08.012en_US
dc.identifier.doi10.1016/j.bbapap.2018.08.012
dc.identifier.issn1570-9639
dc.identifier.urihttps://kr.cup.edu.in/handle/32116/2266
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S157096391830147X?via%3Dihub
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectMolten-globule stateen_US
dc.subjectCrowding agentsen_US
dc.subjectThermal stabilityen_US
dc.subjectCold denaturationen_US
dc.subjectEnthalpy-entropy ploten_US
dc.titleMacromolecular crowding on Dynamics and Thermodynamic Stability of Heme Proteinsen_US
dc.title.journalBiochimica et Biophysica Acta (BBA) - Proteins and Proteomicsen_US
dc.typeArticleen_US
dc.type.accesstypeClosed Accessen_US

Files