Effects of lyotropic anions on thermodynamic stability and dynamics of horse cytochrome c

dc.contributor.authorJain, R.
dc.contributor.authorAgarwal, M.C.
dc.contributor.authorKumar, R.
dc.contributor.authorSharma, D.
dc.contributor.authorKumar, R.
dc.date.accessioned2018-07-14T01:18:43Z
dc.date.accessioned2024-08-13T11:16:22Z
dc.date.available2018-07-14T01:18:43Z
dc.date.available2024-08-13T11:16:22Z
dc.date.issued2018
dc.description.abstractThis paper evaluates the effect of various lyotropic anions (chloride, sulfate, perchlorate, iodide, nitrate, bromide) on the thermodynamic stability and dynamics of native cytochrome c (Cyt c) at pH 7.0. The results of equilibrium and kinetic studies revealed that: (i) at low to intermediate concentrations (? 0.5 M), both chaotropic and kosmotropic anions restrict the dynamics of native protein, (ii) at relatively higher concentrations (? 1.0 M), the denaturing effect of chaotropic anions dominates, which increases the level of structural-fluctuations responsible to unfold the protein according to Hofmeister series (perchlorate > iodide > nitrate > bromide), and (iii) the lyotropic anions affect the thermal and global stability of Cyt c according to Hofmeister series. The m-value was determined from ??G vs [Cosolute] plot and was found to be positive for sulfate and negative for other anions consistent with effect of lyotopic anions on protein stability according to Hofmeister series. ? 2018en_US
dc.identifier.citationJain, R., Agarwal, M. C., Kumar, R., Sharma, D., & Kumar, R. (2018). Effects of lyotropic anions on thermodynamic stability and dynamics of horse cytochrome c. Biophysical Chemistry, 240, 88-97. doi: 10.1016/j.bpc.2018.06.003en_US
dc.identifier.doi10.1016/j.bpc.2018.06.003
dc.identifier.issn0301-4622
dc.identifier.urihttps://kr.cup.edu.in/handle/32116/1307
dc.identifier.urlhttps://www.sciencedirect.com/science/article/abs/pii/S0301462218300875
dc.language.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.titleEffects of lyotropic anions on thermodynamic stability and dynamics of horse cytochrome cen_US
dc.title.journalBiophysical Chemistry
dc.typeArticleen_US

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