Folding of the apolipoprotein A1 driven by the salt concentration as a possible mechanism to improve cholesterol trapping

2014/06/11 by Miguel Ángel Balderas Altamirano, Altamirano, M. A. Balderas, A. Gama Goicochea +3
Biochemistry, Genetics and Molecular Biology · Computer Science · #Computational Drug Discovery Methods #FOS: Physical sciences #Lipid Membrane Structure and Behavior #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft)

paper · pdf · doi:10.48550/arxiv.1406.3003

openalex publication_date 2014/06/11 · openalex created_date 2022/10/03 · openalex updated_date 2026/07/28

Abstract

The folding of the cholesterol trapping apolipoprotein A1 in aqueous solution at increasing ionic strength is studied using atomically detailed molecular dynamics simulations. We calculate various structural properties to characterize the conformation of the protein, such as the radius of gyration, the radial distribution function and the end to end distance. Additionally we report information using tools specifically tailored for the characterization of proteins, such as the mean smallest distance matrix and the Ramachandran plot. We find that two qualitatively different configurations of this protein are preferred, one where the protein is extended, and one where it forms loops or closed structures. It is argued that the latter promote the association of the protein with cholesterol and other fatty acids.

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