Williamson Mike P
School of Biosciences, University of Sheffield, Firth Court, Sheffield S10 2TN, UK.
Life (Basel). 2023 Mar 23;13(4):855. doi: 10.3390/life13040855.
Our understanding of protein binding interactions has matured significantly over the last few years, largely as a result of trying to make sense of the binding interactions of intrinsically disordered proteins. Here, we bring together some disparate ideas that have largely developed independently, and show that they can be linked into a coherent picture that provides insight into quantitative aspects of protein interactions, in particular that transient protein interactions are often optimised for speed, rather than tight binding.
在过去几年里,我们对蛋白质结合相互作用的理解有了显著的成熟,这在很大程度上是由于试图理解内在无序蛋白质的结合相互作用。在这里,我们汇集了一些在很大程度上独立发展的不同观点,并表明它们可以联系成一个连贯的图景,从而深入了解蛋白质相互作用的定量方面,特别是短暂的蛋白质相互作用通常是为速度而非紧密结合而优化的。