DETERMINATION OF 3 DIMENSIONAL STRUCTURES OF MACROMOLECULES IN SOLUTION BY NMR

本实验室的工作重点是测定 通过核磁共振研究溶液中较大蛋白质的三维结构， 特别强调蛋白质-蛋白质、蛋白质-配体和 蛋白质-DNA复合物。 在这方面已经作出了相当大的努力， 发展三维和四维杂波核磁共振， 扩展了NMR作为测定三个- 蛋白质在溶液中的空间结构超出了 常规的二维NMR（约100个残基）对分子进行分析。 150 - 400个残基范围。 一些蛋白质的溶液结构已被确定。 这些包括转录因子GAGA、Are A 和HMG-I/Y与DNA，人硫氧还蛋白与其靶标的复合物 来自Ref和NfkB的位点，以及转座酶的DNA结合结构域 和HIV-整合酶-链球菌蛋白G进行了研究， 多个多芯稳定性和结构完整性 已经检测了链球菌蛋白G的突变体。

Work in this laboratory has been focussed on the determination of three-dimensional structures of larger proteins in solution by NMR, with a particular emphasis on protein-protein, protein-ligand and protein-DNA complexes. A considerable effort has been placed on the developments of three- and four-dimensional heteronuclear NMR to extend the application of NMR as a method for determining three- dimensional structures of proteins in solution beyond the limits of conventional two-dimensional NMR (about 100 residues) to molecules in the 150- to 400- residue range. Solution structures of a number of proteins have been determined. These include the complexes of the transcription factors GAGA, Are A and HMG-I/Y with DNA, complexes of human thioredoxin with its target site from Ref and NfkB, and the DNA binding domains of the transposase and HIV-integrase-Streptococcal protein G have been investigated, and the stability and structural integrity of a number of multiple core mutants of Streptococcal protein G have been examined.