Structural investigation of reaction intermediates in glycolytic aldolases

我们的建议旨在了解称为酶的生物催化剂如何加速活细胞中的化学反应。酶是生命所必需的;没有这些生物催化剂的生命是不可能的。尽管经过多年的研究，生物化学家还没有成功地提供一个全面的描述酶如何完成催化作用。缺少的是关于酶用于加速化学反应的内部机制的详细知识。我们将使用一种我们开创的技术--冻结酶内部的运动--这将使我们能够一步一步地跟踪它的内部工作。为了可视化这些微妙的机制，我们建议使用X射线衍射，它放大了酶的内部原子结构。通过对它们功能的详细研究，我们希望了解酶是如何执行这种惊人的催化壮举的。

Our proposal seeks to understand how the biological catalysts called enzymes speed up chemical reactions in living cells. Enzymes are essential to life; life without these biological catalysts is not possible. Despite years of research, biochemists have not yet succeeded in providing a comprehensive description of how enzymes accomplish catalysis. What is missing is a detailed knowledge about the internal mechanisms that an enzyme uses to speed up chemical reactions. We will use a technique that we pioneered - freezing the motion inside an enzyme - which will allow us to follow its inner workings step by step. To visualise these subtle mechanisms, we propose to use X-ray diffraction, which magnifies the internal atomic structures of enzymes. Through this detailed investigation into their function, we hope to learn how enzymes perform this amazing feat of catalysis.