Stabilization of folding intermediate States from alkaline induced unfolded state of bovine serum fetuin in trifluoroethanol and acetonitrile.
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.
Ahmad
Basir
B
Protein Chemistry & Structural Biology, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
Islam
Zeyaul
Z
Varshney
Ankita
A
Khan
Rizwan Hasan
RH
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
C515594:8-anilino-1-naphthalenesulfonic acid; D000097:Acetonitriles; D000817:Anilino Naphthalenesulfonates; D001798:Blood Proteins; D000509:alpha-Fetoproteins; D014270:Trifluoroethanol; D019791:Guanidine; C032159:acetonitrile