Please use this identifier to cite or link to this item: https://hdl.handle.net/10321/1091
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dc.contributor.authorAnwer, Khalid-
dc.contributor.authorSonani, Ravi-
dc.contributor.authorMadamwar, Datta-
dc.contributor.authorSingh, Parvesh-
dc.contributor.authorKhan, Faez-
dc.contributor.authorBisetty, Krishna-
dc.contributor.authorAhmad, Faizan-
dc.contributor.authorImtaiyaz Hassan, M. D.-
dc.date.accessioned2014-07-15T08:12:23Z-
dc.date.available2014-07-15T08:12:23Z-
dc.date.issued2013-
dc.identifier.citationKhalid Anwer, Ravi Sonani, Datta Madamwar, Parvesh Singh, Faez Khan, Krishna Bisetty, Faizan Ahmad & Md. Imtaiyaz Hassan. 2013. Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies. Journal of Biomolecular Structure and Dynamics. DOI: 10.1080/07391102.2013.855144en_US
dc.identifier.urihttp://hdl.handle.net/10321/1091-
dc.description.abstractThe conformational state of biliproteins can be determined by optical properties of the covalently linked chromophores. Recently determined crystal structure of truncated form of α-subunit of cyanobacterial phycoerythrin (αC-PE) from Phormidium tenue provides a new insight into the structure–function relationship of αC-PE. To compare their stabilities, we have measured urea-induced denaturation transitions of the full length αC-PE (FL-αC-PE) and truncated αC-PE (Tr-αC-PE) followed by observing changes in absorbance at 565 nm, fluorescence at 350 and 573 nm, and circular dichroism at 222 nm as a function of [urea], the molar concentration of urea. The transition curve of each protein was analyzed for ΔGD0, the value of Gibbs free energy change on denaturation (ΔGD) in the absence of urea; m, the slope (=∂ΔGD/∂[urea]), and Cm, the midpoint of the denaturation curve, i.e. [urea] at which ΔGD = 0. A difference of about 10% in ΔGD0 observed between FL-αC-PE and Tr-αC-PE, suggests that the two proteins are almost equally stable, and the natural deletion of 31 residues from the N-terminal side of the full length protein does not alter its stability. Furthermore, normalization of probes shows that the urea-induced denaturation of both the proteins is a two-state process. Folding of both structural variants (Tr-αC-PE and FL-αC-PE) of P. tenue were also studied using molecular dynamics simulations at 300 K. The results show clearly that the stability of the proteins is evenly distributed over the whole structure indicating no significant role of N-terminal residues in the stability of both proteins.en_US
dc.format.extent14 pen_US
dc.language.isoenen_US
dc.publisherTaylor and Fancisen_US
dc.subjectC-phycoerythrinen_US
dc.subjectAMBERen_US
dc.subjectBiliproteinsen_US
dc.subjectChromophoreen_US
dc.subjectProtein denaturationen_US
dc.subjectFolding and stabilityen_US
dc.subjectMolecular dynamicsen_US
dc.titleRole of N-terminal residues on folding and stability of C-phycoerythrin : simulation and urea-induced denaturation studiesen_US
dc.typeArticleen_US
dc.publisher.urihttp://dx.doi.org/10.1080/07391102.2013.855144en_US
dc.dut-rims.pubnumDUT-003933en_US
local.sdgSDG05-
item.fulltextWith Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.openairetypeArticle-
item.grantfulltextopen-
item.cerifentitytypePublications-
Appears in Collections:Research Publications (Applied Sciences)
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