DETERMINATION OF 3 DIMENSIONAL STRUCTURES OF MACROMOLECULES IN SOLUTION BY NMR

该实验室的工作重点是确定 通过 NMR 观察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。 已经付出了相当大的努力 三维和四维异核核磁共振的发展 扩展核磁共振作为测定三-的方法的应用 溶液中蛋白质的维度结构超出了极限 常规二维 NMR（约 100 个残基）对分子 150 至 400 残基范围。 许多蛋白质的溶液结构已被确定。 其中包括转录因子 GAGA、Are A 的复合物 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 结合域 和 HIV-整合酶-链球菌蛋白 G 已被研究，并且 多个多核的稳定性和结构完整性 链球菌 G 蛋白突变体已被检测。

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.