The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated-sheet structure

Smith R. (1985) The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated-sheet structure. FEBS Letters, 183 2: 331-334. doi:10.1016/0014-5793(85)80804-8


Author Smith R.
Title The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated-sheet structure
Journal name FEBS Letters   Check publisher's open access policy
ISSN 0014-5793
Publication date 1985-04-22
Sub-type Article (original research)
DOI 10.1016/0014-5793(85)80804-8
Open Access Status Not yet assessed
Volume 183
Issue 2
Start page 331
End page 334
Total pages 4
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract Sedimentation equilibrium data are shown to be consistent with the existence in solution of an equilibrium between monomers and hexamers of bovine myelin basic protein, without significant accumulation of intermediates. At low concentrations circular dichroism spectra were indicative of an aperiodic coiled secondary structure. At higher concentrations, where the protein self-associates, they showed formation of a β-pleated sheet conformation. At low molar ratios myristoyllysophosphatidylcholine promotes protein self-association and the concomitant conformational transition. The data are consistent with the existence of an equilibrium mixture of relatively unstructured monomers and hexamers in which the polypeptides have a welldefined three-dimensional structure.
Keyword Basic protein
Circular dichroism
Lysophosphatidylcholine
Myelin
Protein self-association
β-pleated sheet
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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Created: Tue, 16 Aug 2016, 11:47:07 EST by System User