Cohen Rachel D, Pielak Gary J
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina, 27599.
Protein Sci. 2017 Mar;26(3):403-413. doi: 10.1002/pro.3092. Epub 2017 Feb 13.
Most knowledge of protein structure and function is derived from experiments performed with purified protein resuspended in dilute, buffered solutions. However, proteins function in the crowded, complex cellular environment. Although the first four levels of protein structure provide important information, a complete understanding requires consideration of quinary structure. Quinary structure comprises the transient interactions between macromolecules that provides organization and compartmentalization inside cells. We review the history of quinary structure in the context of several metabolic pathways, and the technological advances that have yielded recent insight into protein behavior in living cells. The evidence demonstrates that protein behavior in isolated solutions deviates from behavior in the physiological environment.
大多数关于蛋白质结构和功能的知识来源于对溶解在稀释缓冲溶液中的纯化蛋白质进行的实验。然而，蛋白质是在拥挤、复杂的细胞环境中发挥功能的。尽管蛋白质结构的前四个层次提供了重要信息，但要全面理解还需要考虑五级结构。五级结构包括大分子之间的瞬时相互作用，这些相互作用在细胞内提供了组织和区室化。我们在几种代谢途径的背景下回顾了五级结构的历史，以及那些使我们最近对活细胞中蛋白质行为有深入了解的技术进步。证据表明，蛋白质在分离溶液中的行为与在生理环境中的行为不同。
