NMR Studies of Enzyme Conformations

这项研究计划涉及一个密切的调查， 葡萄球菌核酸酶的相关变体 （SNase）与抑制剂和底物的复合物。 这些 研究旨在确定结构的细节 和酶促反应的动力学相关性。 这些 研究将利用一种新型的SNase，SNase， 溶剂可及和无序环已被删除。 初步研究表明，（i）环的缺失 没有大的结构后果;（二）随机 50 - 51位残基的突变可以 产生了具有连续性的结构和活动; (iii)位置43残基可以结合 在50 - 51位随机突变，以研究 （四）基础催化的结构-功能相关性; loop的抑制剂和底物结合的比较 含有和sNase可以提供关于 活性位点相互作用的细节和（v）比较 循环包含和SNAse的灵活性可以提供 关于活性部位灵活性在 催化反应 在这些中使用的主要技术 NMR研究

This research plan involves the investigation of a closely related set of variants of the enzyme Staphylococcal nuclease (SNase) in complexes with inhibitors and substrates. These studies are aimed at determining the details of the structural and dynamical correlates of the enzymatic reaction. These studies will utilize a new type of SNase, SNase, n which the solvent accessible and disordered loop has been deleted. Preliminary studies suggest that (i) the deletion of the loop does not have large structural consequences; (ii) by random mutation of residues 50 & 51 a series of proteins can be generated which have continuum of structures and activities; (iii) the residue at position 43 can be varied in conjunction with random mutation at positions 50 & 51 to investigate the structure-function correlates of basic catalysis; (iv) the comparison of the inhibitor and substrate binding of loop containing and sNase could offer important information about the details of active site interactions and (v) the comparison of the flexibility of loop containing and SNAse may offer information about the role of active site flexibility on the catalytic reaction. the major technique to be used in these studies in NMR.