Secondary structure of pig skin proteodermatan sulfate: a perspective from Raman spectroscopic studies in aqueous solution.
Raman spectroscopic studies of pig skin proteodermatan sulfate in H2O are indicative of a well defined secondary structure consisting of alpha-helical, beta-turn, and possibly "random" structures. The above conclusion is surprisingly close to the secondary structure of the "core" protein of pig skin proteodermatan sulfate proposed in the previous paper (V. Renugopalakrishnan et al., Biopolymers 28, 1923-1933, 1989) from FT-IR and CD spectroscopic studies in aqueous solution.
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D000818:Animals; D002807:Chondroitin / Q000031:analogs & derivatives*; D003871:Dermatan Sulfate / Q000031:analogs & derivatives* / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins; D011509:Proteoglycans / Q000032:analysis*; D012867:Skin / Q000032:analysis*; D012996:Solutions; D013059:Spectrum Analysis, Raman / Q000379:methods; D013552:Swine; D014867:Water
D011506:Proteins; D011509:Proteoglycans; D012996:Solutions; C028774:proteodermatan sulfate; D014867:Water; D003871:Dermatan Sulfate; D002807:Chondroitin