Ontology highlight
ABSTRACT:
SUBMITTER: Deng X
PROVIDER: S-EPMC3576090 | biostudies-literature | 2013 Feb
REPOSITORIES: biostudies-literature
Deng Xiaodi X Morris Jamie J Chaton Catherine C Schröder Gunnar F GF Davidson W Sean WS Thompson Thomas B TB
The Journal of biological chemistry 20130103 7
ApoA-IV is an amphipathic protein that can emulsify lipids and has been linked to protective roles against cardiovascular disease and obesity. We previously reported an x-ray crystal structure of apoA-IV that was truncated at its N and C termini. Here, we have extended this work by demonstrating that self-associated states of apoA-IV are stable and can be structurally studied using small-angle x-ray scattering. Both the full-length monomeric and dimeric forms of apoA-IV were examined, with the d ...[more]