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TitleConformations of human apolipoprotein E(263-286) and E(267-289) in aqueous solutions of sodium dodecyl sulfate by CD and 1H NMR.
Journal, issue, pagesBiochemistry, Vol. 35, Page 10358-10366, Year 1996
Publish dateMar 16, 1996 (structure data deposition date)
AuthorsWang, G. / Pierens, G.K. / Treleaven, W.D. / Sparrow, J.T. / Cushley, R.J.
External linksBiochemistry / PubMed:8756691
MethodsNMR (solution)
Structure data

PDB-1oef:
PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR, 5 STRUCTURES AT PH 4.8, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90
Method: SOLUTION NMR

PDB-1oeg:
PEPTIDE OF HUMAN APOE RESIDUES 267-289, NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsAPOLIPOPROTEIN / GLYCOPROTEIN / PLASMA / LIPID TRANSPORT / HDL / VLDL / CHYLOMICRON / SIALIC ACID / HEPARIN-BINDING / DISEASE MUTATION / POLYMORPHISM

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