High resolution 1H NMR spectra of human apolipoprotein C-III2 using DPC to model the lipoprotein environment

Garry W. Buchko, Annett Rozek, Guangshun Wang, Jiri J. Frohlich, Robert J. Cushley

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

While the apolipoproteins play a central biochemical role in lipid transportation and cardiovascular diseases, structural studies of the apolipoproteins have been primarily confined to optical spectroscopies (circular dichroism and fluorescence). Using deuterated dodecylphosphocholine (DPC) to model the lipoprotein environment, we report the acquisition of high resolution 1H NMR spectra for human apolipoprotein C-III2 isolated from the plasma of a type V hyperlipoproteinemic patient. At a peptide:DPC ratio of 1:60 the pKa of His18 was determined to be 6.15 suggesting the residue is solvent accessible.

Original languageEnglish (US)
Pages (from-to)47-54
Number of pages8
JournalProtein and Peptide Letters
Volume4
Issue number1
StatePublished - Dec 1 1997

Fingerprint

Apolipoproteins C
Apolipoproteins
Lipoproteins
Nuclear magnetic resonance
Dichroism
Circular Dichroism
Spectrum Analysis
Cardiovascular Diseases
Fluorescence
Lipids
Plasmas
Peptides
dodecylphosphocholine
Proton Magnetic Resonance Spectroscopy
Optical spectroscopy

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

High resolution 1H NMR spectra of human apolipoprotein C-III2 using DPC to model the lipoprotein environment. / Buchko, Garry W.; Rozek, Annett; Wang, Guangshun; Frohlich, Jiri J.; Cushley, Robert J.

In: Protein and Peptide Letters, Vol. 4, No. 1, 01.12.1997, p. 47-54.

Research output: Contribution to journalArticle

Buchko, Garry W. ; Rozek, Annett ; Wang, Guangshun ; Frohlich, Jiri J. ; Cushley, Robert J. / High resolution 1H NMR spectra of human apolipoprotein C-III2 using DPC to model the lipoprotein environment. In: Protein and Peptide Letters. 1997 ; Vol. 4, No. 1. pp. 47-54.
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