INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR

本实验室的总体研究目标集中在 尽可能完整地描述结构， 溶液中的肽、蛋白质、核酸及其复合物， 主要通过NMR光谱法。 目前特别强调的是 被放置在发展的方法，使调查 更大和复杂的系统，以及提高精度， 这些解决方案的结构可以获得，研究旨在关联 结构和功能，以及旨在研究蛋白质的实验 折页. 已经对几种蛋白质进行了结构研究。 Mu转座酶的这些DNA结合结构域，Mu转座酶的N-末端结构域，Mu转座酶的N-末端结构域，Mu转座酶的N-末端结构域，Mu转座酶的N-末端结构域。 HIV-1整合酶G。 此外，还对一些 蛋白质核酸复合物，包括GAGA、Are A和 HMG-I/Y。 链球菌蛋白G的突变核心文库也具有 制备并表征了结构以及关于 稳定 其中一个最大的系统，其结构，我们确定， NMR是PTS途径的酶I的N-末端结构域。 在 此外，测定了Hpr或EI的结合表面， 研究磷酸化的结构意义。

The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained, studies aimed at correlating structure and function, and experiments aimed at investigating protein folding. Structural studies for several proteins have been carried out. These DNA binding domains of Mu Transposase, the N-terminal domain of HIV-1 integrase G. In addition, work was also carried out on a number of protein nucleic acid complexes, including those of GAGA, Are A and HMG-I/Y. Also mutant core libraries of streptococcal Protein G have been prepared and characterized structurally as well as with respect to stability. One of the largest systems whose structure we determined by NMR is the N-terminal domain of Enzyme I of the PTS pathway. In addition, the binding surface for Hpr ou EI was determined and structural implications of phosphorylation investigated.