Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein

Shyh Yu Shaw, Richard A. Laursen, Marjorie B. Lees

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)306-310
Number of pages5
JournalFEBS Letters
Volume250
Issue number2
DOIs
Publication statusPublished - 1989 Jul 3

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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