Baron M, Norman D G, Campbell I D
Department of Biochemistry, University of Oxford, UK.
Trends Biochem Sci. 1991 Jan;16(1):13-7. doi: 10.1016/0968-0004(91)90009-k.
As the database of protein sequences grows it is becoming apparent that many proteins are constructed from relatively few modular units that appear many times. Determination of the three-dimensional structure of such modules by NMR has been possible due to their production in relatively large quantities by recombinant DNA techniques. The knowledge gained about the structure of individual modules can then be used to predict their properties in a variety of intact proteins.
随着蛋白质序列数据库的不断增长,越来越明显的是,许多蛋白质是由相对较少的模块化单元构建而成,这些单元会多次出现。由于通过重组DNA技术能够大量生产此类模块,因此利用核磁共振(NMR)确定其三维结构成为可能。随后,所获得的关于单个模块结构的知识可用于预测它们在各种完整蛋白质中的特性。