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

Title: Monitoring Protein Folding and Unfolding Pathways through Surface Hydrophobicity Changes Using Fluorescence and Circular Dichroism Spectroscopy
Authors: Lamba, J
Paul, S
Hasija, V
Aggarwal, R
Chaudhuri, T K
Keywords: surface hydrophobicity
protein unfolding
folding intermediate
fluorescence and circular dichroism spectroscopy
extrinsic fluorescence spectroscopy
Issue Date: 2009
Publisher: Pleiades
Citation: Biochemistry (Moscow) Volume 74, Issue 4, April 2009, Pages 393-398
Abstract: In 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 fr...
URI: http://dx.doi.org/10.1134/S0006297909040063
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