INVESTIGATIONS OF MACROMOLECULAR STRUCTURES AND DYNAMICS IN SOLUTION BY NMR

本实验室的总体研究目标是 尽可能完整地描述这些结构 肽、蛋白质、核酸和它们的复合物在溶液中， 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 将结构和功能联系起来， 研究蛋白质折叠 已经对几种蛋白质进行了结构研究。 这些 包括NfkB和Ref-a，人硫氧还蛋白与其靶复合物 Mu转座酶的DNA结合结构域的DNA结合位点， HIV-1整合酶的结构域，以及 链球菌蛋白G 此外，链球菌蛋白G的突变核心文库具有 在结构上以及在 稳定 还对一些蛋白质核酸进行了研究。 酸络合物，包括GAGA、Are A和HMG-I/Y的酸络合物。

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.