Conformation and aggregation of bovine myelin proteins |
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Authors: | R E Block A H Brady S Joffe |
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Institution: | Papanicolaou Cancer Research Institute Miami, Florida 33123 USA;Departments of Medicine and Biochemistry University of Miami School of Medicine, Miami, Florida 33152 USA;Department of Neurology University of Miami School of Medicine, Miami, Florida 33152 USA |
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Abstract: | CD and PMR spectra were obtained on three major protein fractions of bovine CNS myelin: the basic A-1 protein, the Folch-Lees proteolipid apoprotein (APL), and the Wolfgram proteolipid protein (WPP). Most PMR peaks of the A-1 broadened on going from D2O to salt solutions or to 100% 2-Chloroethanol (2-CE). CD spectra showed no α-helix in water or salt solutions, but showed 42% in 2-CE. The APL showed no PMR in D2O, but did show aromatic amino acid peaks in 1.5% SDS. CD spectra showed 37% α-helix in both cases. The PMR of the WPP in 1.5% SDS showed aromatic amino acids, and the CD showed <20% α-helix. All three proteins showed sharp PMR spectra in trifluoroacetic acid with α-CH chemical shifts characteristic of random coils. It was concluded that the A-1 and the APL aggregate. |
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