title: Stabilization of folding intermediate States from alkaline induced unfolded state of bovine serum fetuin in trifluoroethanol and acetonitrile.
abstract: The conformation of bovine serum fetuin (BSF) was examined over the pH 7.0-12.9 regions by circular dichroism, intrinsic fluorescence and ANS binding. We observed that at higher pH, BSF exists in alkaline unfolded state. Our results provided evidence that correlates simultaneous formation of secondary structure followed by accumulation of hydrophobic clusters.
authors.affiliation: Protein Chemistry & Structural Biology, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
authors.forename: Basir
authors.initials: B
authors.lastname: Ahmad
authors.forename: Zeyaul
authors.initials: Z
authors.lastname: Islam
authors.forename: Ankita
authors.initials: A
authors.lastname: Varshney
authors.forename: Rizwan Hasan
authors.initials: RH
authors.lastname: Khan
mesh_terms: D000097:Acetonitriles / Q000737:chemistry; D000817:Anilino Naphthalenesulfonates; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism; D019791:Guanidine; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008856:Microscopy, Fluorescence; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D014270:Trifluoroethanol / Q000737:chemistry; D000509:alpha-Fetoproteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: C515594:8-anilino-1-naphthalenesulfonic acid; D000097:Acetonitriles; D000817:Anilino Naphthalenesulfonates; D001798:Blood Proteins; D000509:alpha-Fetoproteins; D014270:Trifluoroethanol; D019791:Guanidine; C032159:acetonitrile