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- W2042200755 abstract "The existence of disulfide crosslinks limits the number of possible folded structures a protein can assume. Thus localization of disulfide and thiol groups is a key to understanding the conformation and orientation of myelin proteolipid protein (PLP) in the myelin membrane. [14C]Carboxamidomethylated PLP was fragmented with chymotrypsin, and the resulting mixture was partially separated by reversed-phase HPLC. Purified 14C-labeled peptides and a disulfide containing peptide were characterized by amino acid analysis. These experiments showed that Cys-32 and Cys-34 are free thiols, and are presumably on the interior of the cell or within the membrane bilayer, and that Cys-200 and Cys-219 are joined by a disulfide bond, and are probably located on the extracellular face of the membrane. Sequence analysis experiments indicate that Cys-5, Cys-6 and Cys-9 are linked by disulfides, probably to other parts of the protein on the extracellular face of the membrane." @default.
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- W2042200755 date "1989-07-03" @default.
- W2042200755 modified "2023-09-26" @default.
- W2042200755 title "Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein" @default.
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- W2042200755 doi "https://doi.org/10.1016/0014-5793(89)80744-6" @default.
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