title: pH-dependent conformational transitions in conalbumin (ovotransferrin), a metalloproteinase from hen egg white.
abstract: Acid unfolding pathway of conalbumin (CA), a monomeric glycoprotein from hen egg white, has been investigated using far- and near-UV CD spectroscopy, intrinsic fluorescence emission, extrinsic fluorescence probe 1-anilino-8-napthalene sulfonate (ANS) and dynamic light scattering (DLS). We observe pH-dependent changes in secondary and tertiary structure of CA. It has native-like α-helical secondary structure at pH 4.0 but loss structure at pH 3.0. The CA existed exclusively as a pre-molten globule state and molten globule state in solution at pH 4.0 and pH 3.0, respectively. The effect of pH on the conformation and thermostability of CA points toward its heat resistance at neutral pH. DLS results show that MG state existed as compact form in aqueous solutions with hydrodynamic radii of 4.7 nm. Quenching of tryptophan fluorescence by acrylamide further confirmed the accumulation of an intermediate state, partly unfolded, in-between native and unfolded states.
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202 002, India.
authors.forename: Gulam
authors.initials: G
authors.lastname: Rabbani
authors.forename: Ejaz
authors.initials: E
authors.lastname: Ahmad
authors.forename: Nida
authors.initials: N
authors.lastname: Zaidi
authors.forename: Rizwan Hasan
authors.initials: RH
authors.lastname: Khan
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D000818:Animals; D002645:Chickens; D003207:Conalbumin / Q000737:chemistry* / Q000378:metabolism; D057446:Hydrodynamics; D006863:Hydrogen-Ion Concentration; D045726:Metalloproteases / Q000737:chemistry* / Q000378:metabolism; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D013057:Spectrum Analysis
chemical_list: D000817:Anilino Naphthalenesulfonates; D003207:Conalbumin; C027132:1-anilino-8-naphthalenesulfonate; D045726:Metalloproteases