Proceedings of the National Academy of Sciences · 1984 · 137 citations · 20 references
Natural SciencesBiochemistryBiophysicsMembrane BiochemistryMembrane BiophysicsMolecular NeuroscienceBiological MembranesLipid Bilayer StructureLipid BilayersMembrane DomainsMembrane OrganizationMembrane ProteinsLipid Bilayer MembranesLipid Bilayer OrganizationMembrane Domain OrganizationMembrane Protein DomainsMembrane-spanning DomainsMyelin LipidsMyelin ProteinsMyelin Sheath Structure
A model, based on amino acid sequence data, is proposed for the organization of the myelin proteolipid in myelin membrane. The model has three distinctive features: three trans-membrane segments that traverse the lipid bilayer, two cis-membrane domains that enter and exit the same side of the membrane, and a highly charged segment resembling myelin basic protein on the cytoplasmic side of the membrane. It is proposed that the cis-membrane domain(s) can promote the formation and stabilization of the multilamellar myelin structure by hydrophobic interaction with the apposite bilayer across the extracellular space.
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Principles of protein structure
Journal of Steroid Biochemistry · 1980 · 1.1K citations
A Partial Determination by X-ray Methods, and its Correlation with Chemical Data
J Kendrew, H.C. Watson, B. Strandberg et al. · Nature · 1961 · 485 citations
Path of the polypeptide in bacteriorhodopsin.
Donald M. Engelman, Richard A. Henderson, A. McLachlan et al. · Proceedings of the National Academy of Sciences · 1980 · 366 citations · Full text