Dissertation/Thesis Abstract

Insight in the structure of lipid-bound Locusta migratoria apolipophorin III: A proteolysis study
by Wu.Xinping, M.S., California State University, Long Beach, 2012, 79; 1522271
Abstract (Summary)

Apolipophorin III (apoLp-III) is an insect-derived exchangeable apolipoprotein. The structure of lipid-free apoLp-III is an up-and-down helix bundle consisting of five helices connected by short loops. A high-resolution structure of the physiologically active, lipid-bound form of apoLp-III is not available to date. The lipid-bound apoLp-III is proposed to adapt an antiparallel, fully extended conformation, which surrounds the periphery of the lipid-bilayer in discoidal lipid-protein complexes. This study aims to gain insight into the structure of lipid-bound apoLp-III by proteolysis with trypsin, chymotrypsin, endoproteinase Glu-C and elastase. All four proteases completely cleaved lipid-free apoLp-III. In apoLp-III ยท dimyristoylphosphatidylcholine nanodiscs, lipid-bound apoLp-III was protected by phospholipids and not susceptible to the proteases, except for endoproteinase Glu-C. In lipid-bound apoLp-III, E63, E126 and E137 were cleaved by endoproteinase Glu-C. The results indicate that these residues are exposed to the solvent in lipid-bound apoLp-III in nanodiscs.

Indexing (document details)
Advisor: Weers, Paul M. N.
School: California State University, Long Beach
School Location: United States -- California
Source: MAI 51/05M(E), Masters Abstracts International
Subjects: Biochemistry
Publication Number: 1522271
ISBN: 978-1-267-97766-3
Copyright © 2021 ProQuest LLC. All rights reserved. Terms and Conditions Privacy Policy Cookie Policy