Decoding Order and Disorder in Proteins by NMR Spectroscopy.

ABSTRACT: Proteins often have a complex architecture, consisting of both globular ordered domains and intrinsically disordered regions (IDRs). These multidomain proteins pose challenges for traditional structural biology techniques. One major difficulty arises from the dynamic and flexible nature of IDRs, which lack a stable three-dimensional structure. Indeed, this feature further complicates the application of traditional structural biology techniques. Characterizing these systems is typically simplified by isolating individual domains, which can provide valuable insights into the structure and function of specific regions. However, this approach overlooks the interactions and regulatory mechanisms that occur between domains. To capture the full functional and structural complexity of multidomain

SUBMITTER: Bracaglia L 

PROVIDER: S-EPMC12022988 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature