New insight into the self-association of human apolipoprotein A-I.

Abstract excerpt

Apolipoprotein A-I (apoA-I) is a critical plasma protein responsible for high-density lipoprotein formation, playing a vital role in reverse-cholesterol transport. Lipid-free apoA-I has two domains, an N-terminal helix bundle and a structurally less organized C-terminal (CT) region. In solution, apoA-I self-associates, which is mediated by the CT domain. To gain insight into the self-associated state, cysteine...

Topics

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• Apolipoprotein A-I
• Cysteine
• Mutation
• Protein Domains
• Pyrenes
• Spectrometry, Fluorescence