Deeper Insight of the Conformational Ensemble of Intrinsically Disordered Proteins.

ABSTRACT: It is generally known that, unlike structured proteins, intrinsically disordered proteins, IDPs, exhibit various structures and conformers, the so-called conformational ensemble, CoE. This study aims to better understand the conformers that make up the IDP ensemble by decomposing the CoE into groups separated by their radius of gyration, R_g. A common approach to studying CoE for IDPs is to use low-resolution techniques, such as small-angle scattering, and combine those with computer simulations on different length scales. Herein, the well-studied antimicrobial saliva protein histatin 5 was utilized as a model peptide for an IDP; the average intensity curves were obtained from small-angle X-ray scattering; and compared with fully atomistic, explicit water, molecular dynami

SUBMITTER: Svensson O 

PROVIDER: S-EPMC11323008 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature