title: [Study of conformation of serum albumin by FTIR].
abstract: This paper used the FTIR method to study the spectra of bovine serum albumin (BSA) and its solution. The secondary structure and conformation was assigned by FTIR-deconvolution analysis. The result indicated that BSA secondary structure in solid is different from in aqueous solution. As the decrease of BSA concentration from 3.241 x 10(-1) to 4.032 X 10(-2) g X mL(-1), the amide I band components at 1 609.84, 1 633.85,1 653.69, 1 681.16 and 1 694.88 cm(-1) shifted to 1 608. 24, 1 638.36, 1 656.10, 1 674.87 and 1 690.78 cm(-1), respectively, the component at 1 621.50 cm(-1) unchanged.
authors.affiliation: Department of Bio-Chemistry, Hanshan Teacher's College, 521041 Chaozhou.
authors.forename: Y
authors.initials: Y
authors.lastname: Tong
authors.forename: W
authors.initials: W
authors.lastname: Li
authors.forename: Y
authors.initials: Y
authors.lastname: Lin
mesh_terms: D000818:Animals; D002417:Cattle; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D012710:Serum Albumin, Bovine