Ontology highlight
ABSTRACT:
SUBMITTER: Kale S
PROVIDER: S-EPMC6838881 | biostudies-literature | 2019 Nov
REPOSITORIES: biostudies-literature
Kale Seyit S Strickland Madeleine M Peterkofsky Alan A Liu Jian J Tjandra Nico N
Biophysical journal 20191002 9
Proteins interact with one another across a broad spectrum of affinities. Our understanding of the low end of this spectrum, as characterized by millimolar dissociation constants, relies on a handful of cases in which weak encounters have experimentally been identified. These weak interactions away from the specific target binding site can lead toward a higher-affinity complex. Recently, we detected weak encounters between two paralogous phosphotransferase pathways of Escherichia coli, which reg ...[more]