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High-affinity biomolecular interactions are modulated by low-affinity binders.


ABSTRACT: The strength of molecular interactions is characterized by their dissociation constants (KD). Only high-affinity interactions (KD ≤ 10-8 M) are extensively investigated and support binary on/off switches. However, such analyses have discounted the presence of low-affinity binders (KD > 10-5 M) in the cellular environment. We assess the potential influence of low-affinity binders on high-affinity interactions. By employing Gillespie stochastic simulations and continuous methods, we demonstrate that the presence of low-affinity binders can alter the kinetics and the steady state of high-affinity interactions. We refer to this effect as 'herd regulation' and have evaluated its possible impact in two different contexts including sex determ

SUBMITTER: Mukundan S 

PROVIDER: S-EPMC11316740 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature