Abstract:
:In the present study, the formation of one molten globule-like unfolding intermediate of bovine serum albumin (BSA) at pH 11.2 has been established with the help of circular dichroism (CD) spectra, fluorescence spectroscopy and 'phase diagram' approach. Additionally, we have shown the conformational changes occurring in the pH 11.2 intermediate of BSA when it was exposed to different molecular weight polyethylene glycols (PEGs) at varying concentrations. When the pH 11.2 intermediate of BSA was treated by PEG 400 there was induction of secondary and non-native tertiary contacts. In case of PEG 8000 and PEG 20,000, the loss in secondary as well as tertiary structure was observed. PEG 8000 and 20,000 altered the conformation of the pH 11.2 intermediate and resulted in its transition to another intermediate state in which the hydrophobic patches were inaccessible.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Qu P,Wang Y,Wu G,Lu Z,Xu Mdoi
10.1016/j.ijbiomac.2012.04.021subject
Has Abstractpub_date
2012-07-01 00:00:00pages
97-104issue
1-2eissn
0141-8130issn
1879-0003pii
S0141-8130(12)00152-3journal_volume
51pub_type
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