Effects of pH on the Interactions and Conformation of Bovine Serum Albumin: Comparison between Chemical Force Microscopy and Small-Angle Neutron Scattering | |
Li YQ ; Lee JY ; Lal J ; An LJ ; Huang QR* | |
刊名 | journal of physical chemistry b
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2008 | |
卷号 | 112期号:12页码:3797-3806 |
关键词 | MONTE-CARLO-SIMULATION SINGLE-MOLECULE SPECTROSCOPY PROTEINS KINETICS ADHESION CHARGE AFM SURFACTANTS RESOLUTIO |
ISSN号 | 1520-6106 |
通讯作者 | huang qr |
中文摘要 | the conformation of bovine serum albumin (bsa), as well as its interactions with negatively charged mica surfaces in saline solutions of different ph values, have been studied by small-angle neutron scattering (sans) and chemical force microscopy (cfm), respectively. a new approach to extract the contribution of elementary interactions from the statistically averaged force-extension curves through self-consistent fitting was proposed and used to understand the effects of ph on the interactions and conformation of bsa in saline solutions. when ph increases, the sans results reveal that the sizes of bsa molecules increase slightly, while the statistical analysis of the cfm results shows that the averaged pull-off force for the elongation monotonously decreases. the decrease of pull-off force with the increase of ph results from the decrease in the strength of hydrogen bonding and the number of interaction pairs, as well as the slight increase of the strength of van der waals interaction. when ph approaches the isoelectric point (pi) of bsa, results from both sans and cfm suggest a loss of long-range interactions in bsa molecules. our results also suggest that the force-extension curve is mainly contributed by the van der waals interaction. the combination of sans and cfm provides new insight to understand the interactions and conformation of bsa molecules |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000254209300027 |
公开日期 | 2010-04-14 |
内容类型 | 期刊论文 |
源URL | [http://ir.ciac.jl.cn/handle/322003/9723] ![]() |
专题 | 长春应用化学研究所_长春应用化学研究所知识产出_期刊论文 |
推荐引用方式 GB/T 7714 | Li YQ,Lee JY,Lal J,et al. Effects of pH on the Interactions and Conformation of Bovine Serum Albumin: Comparison between Chemical Force Microscopy and Small-Angle Neutron Scattering[J]. journal of physical chemistry b,2008,112(12):3797-3806. |
APA | Li YQ,Lee JY,Lal J,An LJ,&Huang QR*.(2008).Effects of pH on the Interactions and Conformation of Bovine Serum Albumin: Comparison between Chemical Force Microscopy and Small-Angle Neutron Scattering.journal of physical chemistry b,112(12),3797-3806. |
MLA | Li YQ,et al."Effects of pH on the Interactions and Conformation of Bovine Serum Albumin: Comparison between Chemical Force Microscopy and Small-Angle Neutron Scattering".journal of physical chemistry b 112.12(2008):3797-3806. |
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