Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.

ABSTRACT: It is well accepted that HDL has the ability to reduce risks for several chronic diseases. To gain insights into the functional properties of HDL, it is critical to understand the HDL structure in detail. To understand interactions between the two major apolipoproteins (apos), apoA-I and apoA-II in HDL, we generated highly defined benchmark discoidal HDL particles. These particles were reconstituted using a physiologically relevant phospholipid, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) incorporating two molecules of apoA-I and one homodimer of apoA-II per particle. We utilized two independent mass spectrometry techniques to study these particles. The techniques are both sensitive to protein conformation and interactions and are namely: 1) hydrogen deuterium exchange combined

SUBMITTER: Gauthamadasa K 

PROVIDER: S-EPMC3293592 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature