Month: September 2022

SYNERGY CREATES PLASTICITY. "The notion that disordered regions are largely passive is being actively challenged by the idea that they perform diverse functions, and that synergy between structured and disordered regions expands the functional repertoires of proteins." http://science.sciencemag.org/content/337/6101/1460 View in LinkedIn

ABUNDANT DISORDER. "That it is essential to understand the interaction patterns of proteins with large intrinsically disordered segments becomes evident in the light of their abundance in higher eukaryotes (about 30–40% of their proteins contain large disordered segments) and the finding that proteins enriched in disorder are crucial for cellular processes such as transcription and signal transduction." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

CONFORMATIONALLY LOOSE. "Intrinsically disordered segments lack a unique three-dimensional structure, either entirely or in parts, when expressed as autonomous units, and it is assumed that they sample a variety of conformations that are in equilibrium under physiological conditions." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

THREE MODULES. "There appear to be three different modules within intrinsically disordered regions responsible for their functionally promiscuous behaviour: MoRFs (molecular recognition features), SLiMs (small linear motifs) and LCRs (low complexity regions)." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

PROMISCUOUS BINDING. "Of particular interest in the context of protein-protein interaction networks are findings demonstrating that proteins with many or large intrinsically disordered segments often have the ability to bind promiscuously, with promiscuous proteins or protein segments being those that can bind to many different targets." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

FUNCTIONALITY OF PROMISCUOUS BINDING. "These regions allow for functionality such as engaging in the formation of dynamic heteromeric structures which can serve to increase local activity of an enzyme or store a collection of functionally related molecules for later use." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

DESIRABLE TRAIT. "The studies performed on hub proteins in protein-protein interaction networks reveal that proteins with intrinsically disordered regions take on roles in which promiscuity is a desired trait." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

CENTRALITY. "Proteins with intrinsically disordered segments seem to occupy a central position in the interactome." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

DISORDER CONCENTRATION. "Hubs have higher levels of disorder than non-hubs." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

HUB GROUPINGS. "Numerous studies have broken the hub proteins into two separate categories: those that form simultaneous stable complexes with their many interaction partners (party/multi-interface/stable hubs), and those that interact transiently with their partners at separate times (date/singlish-interface/transient hubs). Of these two hub types, only the transiently interacting hubs were found to be enriched in disorder." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn