...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Crystal growth & design >Anisotropic Distribution of Ammonium Sulfate Ions in Protein Crystallization
【24h】

Anisotropic Distribution of Ammonium Sulfate Ions in Protein Crystallization

机译：蛋白质结晶中硫酸铵离子的各向异性分布

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Some proteins are easily crystallized by utilizing ammonium sulfate (AS) as a precipitant, while others are not. To investigate the difference of AS behavior in protein crystallization between both types of proteins, crystals were grown for two proteins in the former type; carbonic anhydrase II (CAII) and myoglobin (Mb), and also for two proteins in the latter one; hen egg white lysozyme (HEWL) and human serum albumin (HSA). In particular, CAII and Mb were crystallized at high AS concentrations around 3.0 M. In contrast, single crystals were grown at a lower AS concentration of 1.2 M both for HEWL and HSA. Molecular dynamics simulations were carried out for all the proteins with calculation models, including AS at the concentrations of the respective crystallization conditions. The motion of the protein during the simulation was reduced in the presence of AS for all the proteins. Ammonium and sulfate ions (AS ions were anisotropically distributed around the protein molecules, especially for the proteins in the former type, CAII and Mb, under the condition of high AS concentrations. The electrostatic potential around CAII and Mb was almost equally divided into the positive and negative areas, and the AS anisotropic distributions observed in the simulations were compatible with the shape of the iso-surface of the electrostatic potential. In contrast, AS ions were sparsely distributed under the low AS concentration for HEWL and HSA. Either positive or negative area of the electrostatic potential was dominant for HEWL and HSA. Hence, the surrounding space of the latter-type protein was not so distinctively polarized as that of the former-type one. AS ions were anisotropically distributed even for HEWL and HSA, when simulations were performed at high AS concentrations corresponding to 2.0 and 3.0 M in precipitant solution. The AS distributions were, however, different between the former-type proteins and the latter-type ones. Two AS dense areas appeared around CAII and Mb, while AS ions were crowded at one area for HEWL and HSA.
机译：通过利用硫酸铵（AS）作为沉淀剂，一些蛋白质易于结晶，而其他蛋白质不是。为了研究两种类型的蛋白质之间的蛋白质结晶行为的差异，将晶体生长前一种蛋白质;碳酸酐酶II（CAII）和肌球蛋白（MB），以及后者中的两种蛋白质;母鸡蛋白溶菌酶（Hewl）和人血清白蛋白（HSA）。特别地，CaII和Mb以高于3.0米的浓度高，在3.0米左右结晶。相反，为HEWL和HSA的浓度低至1.2μm的单晶生长。对具有计算模型的所有蛋白质进行分子动力学模拟，包括在各个结晶条件的浓度下。在所有蛋白质的情况下，在模拟期间蛋白质的运动减少。铵和硫酸盐离子（如离子周围地分布在蛋白质分子周围），特别是在浓度高的情况下为前者类型，CaII和Mb中的蛋白质。CaII和MB周围的静电势几乎将其分成正面在模拟中观察到的负面区域，并且在模拟中观察到的各向异性分布与静电电位的ISO表面的形状相容。相反，当离子稀疏地分布在低至HEWL和HSA的浓度下。正面或阴性静电潜力的区域是Hewl和HSA的主导。因此，后者型蛋白质的周围空间并不像前者型型一样偏振。即使对于Hewl和HSA，离子也是各向异性分布的，当模拟时以高于对应于2.0和3.0μm的沉淀剂溶液的浓度高。然而，作为分布是不同的前者型蛋白质和后者型之间的NT。两种致密的区域出现在Caii和Mb周围，而在Hewl和HSA的一个区域时，随着离子的群体。

著录项

  • 来源
    《Crystal growth & design》 |2019年第11期|共7页
  • 作者

    Kitahara Mariko; Fudo Satoshi; Yoneda Tomoki; Nukaga Michiyoshi; Hoshino Tyuji;

  • 作者单位

    Chiba Univ Grad Sch Pharmaceut Sci Chuo Ku Inohana 1-8-1 Chiba 2608675 Japan;

    Chiba Univ Grad Sch Pharmaceut Sci Chuo Ku Inohana 1-8-1 Chiba 2608675 Japan;

    Chiba Univ Grad Sch Pharmaceut Sci Chuo Ku Inohana 1-8-1 Chiba 2608675 Japan;

    Josai Int Univ Fac Pharmaceut Sci Gumyo 1 Togane Chiba 2838555 Japan;

    Chiba Univ Grad Sch Pharmaceut Sci Chuo Ku Inohana 1-8-1 Chiba 2608675 Japan;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 晶体学;
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号