INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR

本实验室整体研究的目标是围绕 关于对结构的尽可能完整的描述 在溶液中的多肽、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，以及通过 这些溶液结构可以获得哪些，研究的目的是 结构和功能的关联，以及旨在 研究蛋白质折叠。 对几种蛋白质的结构进行了研究。这些 包括NFkB和Ref-A、人硫氧还蛋白与其靶标络合物 从Mu转座酶的DNA结合域开始，DNA结合 HIV-1整合酶的结构域和尿素变性状态 链球菌蛋白G. 此外，链球菌G蛋白的突变核心文库具有 已经做好了准备，并在结构上和尊重上进行了表征 为稳定干杯。还在一些蛋白质核上开展了工作 酸性络合物，包括GAGA的络合物，是A和HMG-I/Y。

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 include NfkB and Ref-a, complexes of human thioredoxin with its target site from DNA binding domains of Mu Transposase, the DNA binding domain of HIV-1 integrase, and the urea denatured state of Streptoccoccal Protein G. In addition, mutant core libraries of streptococcal Protein G have been prepared and characterized structurally as well as with respect to stability. Work is also carried out on a number of protein nucleic acid complexes, including those of GAGA, Are A and HMG-I/Y.