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Please use this identifier to cite or link to this item: http://hdl.handle.net/2080/925

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contributor.authorLamba, J-
contributor.authorPaul, S-
contributor.authorHasija, V-
contributor.authorAggarwal, R-
contributor.authorChaudhuri, T K-
identifier.citationBiochemistry (Moscow) Volume 74, Issue 4, April 2009, Pages 393-398en
description.abstractIn the present study we have investigated the characteristics of folding and unfolding pathways of two model proteins, ovalbumin and ╬▒lactalbumin, monitored through the changes in surface hydrophobicity using fluorescence and circular dichroism spectroscopy. In the unfolding process, it was observed that ovalbumin and ╬▒lactalbumin followed a three state transition pathway involving an intermediate state having high surface hydrophobicity. The intermediate state has also been characterized by circular dichroism spectroscopy, and it was found that the intermediate retained almost the same secondary structure as the native proteins, and therefore it can be referred to as molten globule state. The refolding process was monitored using fluorescence and circular dichroism spectroscopy, and it was observed that the refolding of ╬▒lactalbumin was reversible and proceeded through the accumulation of similar type of intermediates as observed during its unfolding pathway. However, on refolding from the guanidine hydrochloridedenatured state, ovalbumin reached a different folded state.en
format.extent154222 bytes-
subjectsurface hydrophobicityen
subjectprotein unfoldingen
subjectfolding intermediateen
subjectfluorescence and circular dichroism spectroscopyen
subjectextrinsic fluorescence spectroscopyen
titleMonitoring Protein Folding and Unfolding Pathways through Surface Hydrophobicity Changes Using Fluorescence and Circular Dichroism Spectroscopyen
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