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首页> 外文学位 >The physical chemistry underlying the assembly and midpoint potential control in a series of designed protein-maquettes.
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The physical chemistry underlying the assembly and midpoint potential control in a series of designed protein-maquettes.

机译：在一系列设计的蛋白质模型中，装配和中点电位控制所依据的物理化学。

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In nature, oxidoreductase proteins are responsible for many enzymatic processes critical to life. These proteins often rely on the presence of non-proteinaceous cofactors to take part in the enzymatic function. The most common, central to my thesis, is heme B. Depending on the protein environment, this cofactor can take part in functions as diverse as electron transfer (cytochromes), oxygen transport (hemoglobins), oxygen reduction (oxidases), carbon-hydroxylation (oxygenases), and superoxide production (NADH oxidase).;In natural oxidoreductases, determination of the course and rates of heme-protein association, what barriers are encountered, what affinity is achieved, and what are the oxidation-reduction potentials, is critical for understanding the rules of assembly and function of the different activities performed. In the growing field of research attempting to make man-made oxidoreductases, the same understanding is required for progress to be made toward construction of novel enzymes. However, this understanding is still out of reach in natural oxidoreductases because of the immense complexity of natural proteins, while for man-made designs progress has only recently reached a point where an in-depth systematic study can be contemplated. ;My thesis states: Simple non-natural proteins (maquettes) designed from first principles to ligate heme, can be used to uncover the factors derived from the oligomeric and structural state of related maquette and also derived from porphyrin variants of heme B, that govern rates of incorporation and ligation of heme B into a maquette. Maquettes are ideal platforms to demonstrate what aspects of a protein govern heme redox potentials, a key parameter underlying the diversity of hemoprotein functions. ;The findings from my work provide the first views of heme and maquette assembly: spontaneous, rapid and with high affinity association. They also provide a foundation for understanding what controls redox potentials of the heme and perspective on this control. The work offers insight into similar processes in natural oxidoreductases, but the concepts and principles uncovered in this thesis will be vital in the development of novel functions applied in man-made applications in vitro and in vivo.
机译：在自然界中，氧化还原酶蛋白负责许多对生命至关重要的酶促过程。这些蛋白质通常依赖于非蛋白质辅因子的存在来参与酶促功能。在我的论文中，最常见的中心是血红素B。根据蛋白质环境的不同，该辅因子可以参与多种功能，例如电子转移（细胞色素），氧转运（血球蛋白），氧还原（氧化酶），碳羟基化（加氧酶）和超氧化物的产生（NADH氧化酶）。在天然氧化还原酶中，确定血红素-蛋白质缔合的过程和速率，遇到的障碍，实现的亲和力和氧化还原电位是至关重要的了解组装规则和执行的不同活动的功能。在试图制造人造氧化还原酶的不断增长的研究领域中，对于构建新型酶的进展需要相同的理解。然而，由于天然蛋白质的复杂性，对天然氧化还原酶的理解仍然遥不可及，而对于人造设计，直到最近才取得进展，可以进行深入的系统研究。 ；我的论文指出：从最初的原理设计以连接血红素的简单非天然蛋白质（模型），可用于揭示相关模型的寡聚体和结构状态的衍生因子，以及源自血红素B的卟啉变体的因子血红素B掺入和连接到模型中的速率。 Maquettes是展示蛋白质哪些方面控制血红素氧化还原电位的理想平台，血红素氧化还原电位是血红蛋白功能多样性的关键参数。 ；从我的工作中获得的发现提供了血红素和模型组装的最初观点：自发，快速且具有高亲和力。它们还为理解什么控制血红素的氧化还原电位和对该控制的观点提供了基础。这项工作提供了对天然氧化还原酶中类似过程的见解，但本论文中揭示的概念和原理对于开发用于体外和体内人为应用的新型功能至关重要。

著录项

  • 作者

    Solomon, Lee A.;

  • 作者单位

    University of Pennsylvania.;

  • 授予单位 University of Pennsylvania.;
  • 学科 Biophysics General.;Chemistry Biochemistry.
  • 学位 Ph.D.
  • 年度 2013
  • 页码 153 p.
  • 总页数 153
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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