Videler Hortense, Ilag Leopold L, McKay Adam R C, Hanson Charlotte L, Robinson Carol V
The University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK.
FEBS Lett. 2005 Feb 7;579(4):943-7. doi: 10.1016/j.febslet.2004.12.003.
The ability to maintain intact ribosomes in the mass spectrometer has enabled research into their changes in conformation and interactions. In the mass spectrometer, it is possible to induce dissociation of proteins from the intact ribosome and, in conjunction with atomic structures, to understand the factors governing their release. We have applied this knowledge to interpret the structural basis for release of proteins from ribosomes for which no high resolution structures are available, such as complexes with elongation factor G and ribosomes from yeast. We also describe how improvements in technology and understanding have widened the scope of our research and lead to dramatic improvements in quality and information available from spectra of intact ribosomes.
在质谱仪中保持核糖体完整的能力，使得对其构象变化和相互作用的研究成为可能。在质谱仪中，可以诱导蛋白质从完整核糖体上解离，并结合原子结构，了解控制其释放的因素。我们已运用这一知识来解释那些没有高分辨率结构的核糖体释放蛋白质的结构基础，比如与延伸因子G的复合物以及酵母核糖体。我们还描述了技术改进和认识的提高如何拓宽了我们的研究范围，并使完整核糖体光谱的质量和可用信息得到显著改善。
