STRUCTURAL STUDIES OF PROTEIN SUBUNITS

在最广泛的意义上，我们想要确定基本的 蛋白质产生其功能的原理。这 既需要对多肽折叠有准确的了解，也需要对 氨基酸侧链的原子排列及其相关知识 蛋白质的功能成分及其相互作用 与相关的其他分子结合。 我们已经开始了一项关于单抗的研究。 中和鼻病毒和芒果病毒。一直以来 可能生长一种大的、高衍射率的晶体 与人结合部位的抗原结合组分(Fab) 鼻病毒14(HRV14)已经被仔细绘制了地图。它也一直是 可以生长FAB和相应的HRV14的晶体 多肽。合适的对接实验可能会提示 单抗结合引起的构象变化 中和。 磷酸葡萄糖变位酶(PGM)和乳酸脱氢酶的研究 (LDH)将继续。随着精致结构的出现， 我们计划研究PGM的酶-底物复合体和 嗜热菌B.stearthermophilus LDH.

In the broadest sense, we would like to determine the fundamental principles from which proteins derive their function. This requires both a precise knowledge of polypeptide fold and the atomic arrangements of amino acid side chains and knowledge of the functional components of the protein and their interaction with relevant other molecules. We have initiated an investigation of monoclonal antibodies (Mab) that neutralize rhinoviruses and Mengo viruses. It has been possible to grow large and highly diffracting crystals of one antigen binding fraction (Fab) whose binding site on human rhinovirus 14 (HRV14) has been carefully mapped. It has also been possible to grow crystals of the Fab and corresponding HRV14 peptide. Suitable docking experiments may then suggest the conformational changes produced by Mab binding to cause neutralization. Studies on phosphoglucomutase (PGM) and lactate dehydrogenase (LDH) are to continue. With the availability of refined structures, we plan to study enzyme-substrate complexes for PGM and the thermophile B. stearothermophilus LDH.