期刊
JOURNAL OF COLLOID AND INTERFACE SCIENCE
卷 363, 期 2, 页码 579-584出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2011.07.043
关键词
Equilibrium clusters; Salt-free lysozyme solutions; Short-range attraction and weak long-range repulsion effective potential; Scattering experiments
资金
- Office of Research & Development, Curtin University of Technology [CRF10084]
- Polish Ministry of Science and Higher Education [NN 202 006034]
- European Regional Development Fund within Innovative Economy Operational Programme Grants for innovation.
We have studied the structure of salt-free lysozyme at 293 K and pH 7.8 using molecular simulations and experimental SAXS effective potentials between proteins at three volume fractions, phi = 0.012, 0.033, and 0.12. We found that the structure of lysozyme near physiological conditions strongly depends on the volume fraction of proteins. The studied lysozyme solutions are dominated by monomers only for phi <= 0.012; for the strong dilution 70% of proteins are in a form of monomers. For phi = 0.033 only 20% of proteins do not belong to a cluster. The clusters are mainly elongated. For phi = 0.12 almost no individual particles exits, and branched, irregular clusters of large extent appear. Our simulation study provides new insight into the formation of equilibrium clusters in charged protein solutions near physiological conditions. (C) 2011 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据