title: Secondary structure of a core protein from pig skin proteodermatan sulfate: CD and Fourier transform IR spectroscopic studies in solution.
abstract: The secondary structure of a 38 kDa core protein from pig skin proteodermatan sulfate (PDS), was investigated in solution using CD and Fourier transform (FT) ir spectroscopy. Both techniques generally have provided complementary data on the secondary structures of proteins. CD spectral analysis has shown that the core protein contains 60% beta-turn and alpha-helical structures, the rest being "unordered" structure. FT ir data do not permit calculation of quantitative contributions of substructures, at the present time, to the overall secondary structure of the core protein. CD spectrum of the intact PDS is similar to the core protein CD spectrum.
authors.forename: V
authors.initials: V
authors.lastname: Renugopalakrishnan
authors.forename: S P
authors.initials: SP
authors.lastname: Damle
authors.forename: P M
authors.initials: PM
authors.lastname: Horowitz
authors.forename: S
authors.initials: S
authors.lastname: Moore
authors.forename: T B
authors.initials: TB
authors.lastname: Hutson
authors.forename: J D
authors.initials: JD
authors.lastname: Gregory
mesh_terms: D000818:Animals; D002807:Chondroitin / Q000031:analogs & derivatives*; D002942:Circular Dichroism; D003871:Dermatan Sulfate / Q000031:analogs & derivatives* / Q000032:analysis; D005583:Fourier Analysis; D011487:Protein Conformation; D011506:Proteins / Q000302:isolation & purification; D011509:Proteoglycans / Q000032:analysis*; D012867:Skin / Q000032:analysis*; D013055:Spectrophotometry, Infrared / Q000379:methods; D013552:Swine
chemical_list: D011506:Proteins; D011509:Proteoglycans; C028774:proteodermatan sulfate; D003871:Dermatan Sulfate; D002807:Chondroitin