DETERMINATION OF 3 DIMENSIONAL STRUCTURES OF MACROMOLECULES IN SOLUTION BY NMR

这个实验室的工作一直集中在测定 用核磁共振研究较大蛋白质在溶液中的三维结构 特别强调蛋白质-蛋白质、蛋白质-配体和 蛋白质-DNA复合体。已经在这方面付出了相当大的努力 三维和四维异核核磁共振的研究进展 扩大核磁共振作为测定三种有机化合物的方法的应用 超出极限的蛋白质在溶液中的空间结构 常规二维核磁共振(约100个残基)在分子中的应用 150到400个残留物的范围。 测定了一些蛋白质的溶液结构。 这些包括转录因子GagA的复合体，是A 和HMG-I/Y与DNA、人硫氧还蛋白与其靶标的络合物 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G蛋白的研究，以及 多个多核的稳定性和结构完整性 对链球菌G蛋白的突变体进行了检测。

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.