Winston R L, Fitzgerald M C
Scripps Research Institute, La Jolla, California 92037, USA.
Mass Spectrom Rev. 1997 Jul-Aug;16(4):165-79. doi: 10.1002/(SICI)1098-2787(1997)16:4<165::AID-MAS1>3.0.CO;2-F.
Proteins have evolved to carry out very specific functions within the cell by interacting with a diverse set of biomolecules. Understanding how a protein's higher order structure relates to its function is important for defining the molecular basis of these interactions. In recent years, mass spectrometry has become an important tool for dissecting protein structure and function. Using electrospray ionization (ESI)- and matrix-assisted laser desorption/ionization (MALDI)-based approaches, it has been possible to monitor protein folding, characterize noncovalent protein complexes, and assess the contribution of individual amino acid residues to a protein's function. Here, it is our goal to summarize these approaches and highlight recent, biologically relevant applications where mass spectrometry has provided unique insight into the mysteries of protein structure and function.
蛋白质通过与多种生物分子相互作用,在细胞内进化以执行非常特定的功能。了解蛋白质的高级结构如何与其功能相关,对于定义这些相互作用的分子基础很重要。近年来,质谱已成为剖析蛋白质结构和功能的重要工具。使用基于电喷雾电离(ESI)和基质辅助激光解吸/电离(MALDI)的方法,已经能够监测蛋白质折叠、表征非共价蛋白质复合物,并评估单个氨基酸残基对蛋白质功能的贡献。在这里,我们的目标是总结这些方法,并突出最近在生物学上相关的应用,其中质谱为蛋白质结构和功能的奥秘提供了独特的见解。