Contribution of alpha helix formation in human plasma apolipoproteins to their enthalpy of association with phospholipids.

J. B. Massey, A. M. Gotto, H. J. pownall

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

The human plasma apolipoproteins, apo-A-II and apo-C-III, assocaite with phospholipid with a concurrent increase in alpha helical structure of the apoprotein and an exothermic enthalpy of association. A linear correlation of the increase in alpha helical structure and the exothermic enthalpy of association gave a value of -1.3 kcal/mol of amino acid residues converted from a random coil to an alpha helical structure. This value is very close to that of alpha helix formation by charged polyamino acids (-1.2 kcal/mol) and suggests that amino acid side chains contribute little or no heat to the random coil leads to alpha helix transition in the plasma apolipoproteins. In the absence of a change in alpha helix in the apolipoproteins studied here, the enthalpy of association is practically nil, suggesting that alpha helix formation is a major enthalpic contribution to the total free energy of lipid-apolipoprotein association.

Original languageEnglish (US)
Pages (from-to)9559-9561
Number of pages3
JournalJournal of Biological Chemistry
Volume254
Issue number19
StatePublished - Oct 10 1979

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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