化学
结晶学
磷脂
Crystal(编程语言)
聚类分析
晶体学点群
化学物理
热力学
晶体结构
物理
膜
生物化学
计算机科学
机器学习
程序设计语言
作者
Sidney Winford,M. N. Tobin,Eitan Gross
标识
DOI:10.1016/j.jcrysgro.2011.12.059
摘要
In condensed matter physics the geometry of a crystal is determined by the mechanism of condensation. In biology, the link between clustering mechanisms and the shape of a protein crystal is not well defined. To gain more insight into the problem, we studied clustering of apolipoprotein A-I (apo A-I) on a solid surface using AFM. The amyloidogenic protein apo A-I is the main protein component of high density lipoprotein and thus reduces the risk of atherosclerosis. We found that apo A-I clustered to form nano-scale, symmetrical clusters on mica. Statistical analysis of size distribution for several thousand clusters suggested that the clustering reaction followed a non-cooperative kinetic scheme characterized by a single equilibrium constant of 0.92·106 M−1 and a change in free energy (ΔG) of −0.03 kJ mole−1/residue. This is close to ΔG of−0.04 kJ mole−1/residue for apo A-I binding to phospholipid membrane; and 30-fold smaller than ΔG for β-amyloid formation by apo A-I. The high symmetry of the clusters is consistent with an isotropic diffusion coefficient of protein monomers on the surface of the substrate. This previously unrecognized link between protein clustering mechanism and the symmetry of the growth pattern may have important implications in medicine, pharmaceutics and polymer science.
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