Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions

Title: Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions

Volume: 17 Issue: 1

Author(s): M. A. Ansari, S. Zubair, S. M. Atif, M. Kashif, N. Khan, M. Rehan, T. Anwar, A. Iqbal and M. Owais

Affiliation:

Keywords: Lysozyme, secondary structure, molten globule

Abstract: In the present study, we elucidated the effect of potassium salts on alkali denatured hen egg white lysozyme (EC 3.2.1.17) using intrinsic/extrinsic fluorescence as well circular dichroism (CD) spectroscopic methods. Intrinsic fluorescence studies revealed that various potassium salts mediate stabilization of lysozyme against alkali denaturation. Far and near UV CD spectrum studies, showed that 2M KCl induced appreciable amount of secondary structure with minimum tertiary contacts in lysozyme at pH 12.6. Acrylamide quenching studies suggest that at pH 12.6, the presence of 2M KCl causes reduced accessibility of the quencher to tryptophan residues of the protein presumably because of its compact conformation. In summary, the results of present study suggest that lysozyme attains a compact folded intermediate with molten globule like characteristics at alkaline pH in presence of potassium chloride.

Cite this article as:

Ansari A. M., Zubair S., Atif M. S., Kashif M., Khan N., Rehan M., Anwar T., Iqbal A. and Owais M., Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions, Protein & Peptide Letters 2010; 17 (1) . https://dx.doi.org/10.2174/092986610789909502

DOI https://dx.doi.org/10.2174/092986610789909502	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305