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首页> 外文学位 >Effect of divalent cations and solubilizers in apoferritin and gamma d-crystallin solutions: Nucleation, crystallization and light scattering studies.
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Effect of divalent cations and solubilizers in apoferritin and gamma d-crystallin solutions: Nucleation, crystallization and light scattering studies.

机译：载铁蛋白和γd-晶状体蛋白溶液中二价阳离子和增溶剂的作用：成核，结晶和光散射研究。

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摘要

Crystallization of proteins in the human body can lead to the development of diseases such as sickle cell anemia and cataract. Understanding the processes involved in protein crystallization can help us gain a better understanding of such diseases. Furthermore, protein crystallization is necessary for protein structure resolution which is the first step towards determination of protein function. This is important since resolution of protein structure is the first step towards establishing structure/function relations, and possibly at performing specific structural modifications that may change the function in desirable directions. Another important application of protein crystallization is in downstream processing in the pharmaceutical industry where it is used for separation and as a final purification step. The present study increases knowledge of interactions between protein molecules during crystallization and hence the crystallization process.;Crystallization of a lens protein, human gamma D-crystallin (HGD), was studied in relation to cataract formation. The crystallization habits of this protein were determined in the presence of divalent cations which are found at elevated concentrations in cataractous lenses. Results indicate that the divalent cations studied enhance crystallization of HGD.;A thermodynamic property, the osmotic second virial coefficient, was measured in protein solutions and its value was correlated with the occurrence of crystallization. It was found that the second virial coefficient successfully predicted crystallization of HGD. A new method was developed for indirect measurement of the second virial coefficient using dynamic light scattering. This new method is more robust and efficient than the traditional static light scattering method.;Finally the ability of solubilizers to prevent crystallization of proteins was studied. A commercial solubilizer, NDSB-201, was found to increase the energy barrier to nucleation. Although this did not prevent crystallization, it resulted in fewer and smaller crystals being obtained. The naturally occurring alpha A-crystallin was a superior solubilizer to NDSB-201, as it suppressed aggregation and prevented crystallization of HGD under conditions for which NDSB-201 did not.;The findings in the present study provide insight into the processes by which protein crystallization occurs. Using the second virial coefficient to assess whether a protein will crystallize out of solution, approaches for retardation and prevention of protein crystallization, and implications for future research, are discussed.
机译：人体中蛋白质的结晶可导致镰状细胞性贫血和白内障等疾病的发展。了解蛋白质结晶过程可以帮助我们更好地了解此类疾病。此外，蛋白质结晶对于蛋白质结构解析是必需的，这是确定蛋白质功能的第一步。这很重要，因为蛋白质结构的解析是建立结构/功能关系的第一步，并且可能是执行可能在所需方向上改变功能的特定结构修饰。蛋白质结晶的另一个重要应用是在制药行业的下游加工中，用于分离和最终纯化步骤。本研究增加了结晶过程中蛋白质分子之间相互作用的知识，因此也增加了结晶过程。研究了晶状体蛋白质人类γD-晶状蛋白（HGD）的结晶与白内障形成的关系。该蛋白质的结晶习性是在二价阳离子存在下测定的，该二价阳离子在白内障晶状体中浓度升高。结果表明所研究的二价阳离子增强了HGD的结晶。;在蛋白质溶液中测量了热力学性质，即渗透第二维里系数，其值与结晶的发生有关。发现第二病毒系数成功地预测了HGD的结晶。开发了一种使用动态光散射间接测量第二维里系数的新方法。这种新方法比传统的静态光散射方法更鲁棒，更有效。最后，研究了增溶剂防止蛋白质结晶的能力。发现商业增溶剂NDSB-201可增加成核的能垒。尽管这不能防止结晶，但是却导致获得的晶体越来越少。天然存在的αA-晶状体蛋白是NDSB-201的优异增溶剂，因为它在NDSB-201没有的条件下抑制聚集并阻止了HGD的结晶。本研究的发现提供了深入了解蛋白质形成过程的信息。发生结晶。讨论了使用第二病毒系数评估蛋白质是否会从溶液中结晶出来，讨论了阻碍和防止蛋白质结晶的方法，以及对未来研究的意义。

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  • 作者

    Nwanosike, Quinta Mgbeke.;

  • 作者单位

    Georgia Institute of Technology.;

  • 授予单位 Georgia Institute of Technology.;
  • 学科 Engineering Chemical.
  • 学位 Ph.D.
  • 年度 2009
  • 页码 272 p.
  • 总页数 272
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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