title: Denaturation studies of P2 protein using circular dichroism.
abstract: The denaturation process of P2 protein has been investigated using circular dichroism spectroscopy. The influence of temperature and the presence of urea were the factors investigated. Increasing temperature causes the destruction of beta-structure, while helical structure remains intact even at relatively high temperatures. Increasing the urea concentration destroyed all forms of secondary structure in P2 and the study also supports the model of a stepwise denaturation process of the protein.
authors.affiliation: Department of Materials Science, University of Technology, Sydney, Australia.
authors.forename: B H
authors.initials: BH
authors.lastname: Stuart
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D018996:Myelin P2 Protein / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013696:Temperature; D014508:Urea / Q000494:pharmacology
chemical_list: D018996:Myelin P2 Protein; D014508:Urea