Interpreting Transient Interactions of Intrinsically Disordered Proteins.

ABSTRACT: The flexible nature of intrinsically disordered proteins (IDPs) gives rise to a conformational ensemble with a diverse set of conformations. The simplest way to describe this ensemble is through a homopolymer model without any specific interactions. However, there has been growing evidence that the conformational properties of IDPs and their relevant functions can be affected by transient interactions between specific and even nonlocal pairs of amino acids. Interpreting these interactions from experimental methods, each of which is most sensitive to a different distance regime referred to as probing length, remains a challenging and unsolved problem. Here, we first show that transient interactions can be realized between short fragments of charged amino acids by generating conformational e

SUBMITTER: Wohl S 

PROVIDER: S-EPMC10038935 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature