Structural and Functional Relevance of Charge Based Transient Interactions inside Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) perform a wide range of biological functions without adopting stable, well-defined, three-dimensional structures. Instead, IDPs exist as dynamic ensembles of flexible conformations, traditionally thought to be governed by weak, nonspecific interactions, which are well described by homopolymer theory. However, recent research highlights the presence of transient, specific interactions in several IDPs, suggesting that factors beyond overall size influence their conformational behavior. In this study, we investigate how the spatial arrangement of charged amino acids within IDP sequences shapes the prevalence of transient, specific interactions. Through a series of model peptides, we establish a quantitative empirical relationship between the fraction o

SUBMITTER: Wohl S 

PROVIDER: S-EPMC11565980 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature