INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR

本实验室整体研究的目标是围绕 实现对结构的尽可能完整的描述 溶液中的多肽、蛋白质、核酸及其络合物， 主要是通过核磁共振光谱分析。目前特别强调的是 致力于开发方法，以允许调查 更大、更复杂的系统，以及提高其精度 这些溶液结构是可以获得的，研究的目的是关联 结构和功能，以及旨在研究蛋白质的实验 折叠。对几种蛋白质的结构进行了研究。 Mu转座酶的这些DNA结合域，即Mu转座酶的N-末端结构域 艾滋病毒-1整合酶G。此外，还开展了一些 蛋白质核酸复合体，包括GAGA的复合体，是A和 HMG-I/Y。链球菌蛋白G的突变核心文库也有 已经准备好并在结构上以及关于 稳定性。最大的系统之一，它的结构是由 核磁共振是PTS途径中酶I的N端结构域。在……里面 此外，还测定了HPR OUEI的结合面，并 研究了磷酸化的结构含义。

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.