Article
Structure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation.
Biochemistry - 31 Jan 2006
Gorshkova Irina N, Liu Tong, Kan Horng-Yuan, Chroni Angeliki, Zannis Vassilis I, Atkinson David
Abstract excerpt
To identify residues and segments in the central region of apolipoprotein A-I (apoA-I) that are important for the protein structure and stability, we studied the effects of four double charge ablations, D102A/D103A, E110A/E111A, R116V/K118A, and R160V/H162A, and two deletion mutations, Delta(61-78) and Delta(121-142), on the conformation and stability of apoA-I in the lipid-free state and in reconstituted...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
