DETERMINATION OF 3 DIMENSIONAL STRUCTURES OF MACROMOLECULES IN SOLUTION BY NMR

该实验室的工作重点是测定 通过NMR分析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 配合物 在开发方面投入了相当大的努力， 三维和四维杂波NMR，以扩展应用 NMR作为确定三维结构的方法 蛋白质在溶液中超越了传统的二维限制 150至400个残基范围内的分子的NMR（~ 100个残基），以及 为了开发新的NMR方法用于确定长范围优先级顺序， 包括异源关联数据对扩散的依赖性 各向异性和使用剩余的dipl耦合所产生的磁 磁化率各向异性 一些蛋白质的溶液结构 已经确定。 这些包括转录的复合体 因子GAGA、Are A和HMG-I/Y与DNA、DNA MuA结合结构域 转座酶的30 kDa（259个残基）N末端结构域 I的PTS途径，gp 41的44 kDa胞外域，和N-末端 HIV-1整合酶的结构域。

Work in this laboratory has been focused 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 development 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 (-100 residues) to molecules in the 150- to 400- residue range, and to develop new NMR methods for determining long range order of priority, including the dependence of heteronuclear relevation data on diffusion anisotropy and the use of residual dipl couplings arising from magnetic susceptibility anisotropy. 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, the DNA MuA binding domains of the transposase, the 30 kDa (259 residue) N terminal domain of Enzyme I of the PTS pathway, the 44 kDa ectodomain of gp41, and the N-terminal domain of HIV-1 integrase.