HACANCOi: a new H^α-detected experiment for backbone resonance assignment of intrinsically disordered proteins.

ABSTRACT: Unidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T₂) relaxation times allowing sophisticated coherence transfer pathway selection in comparison to folded proteins. ¹H^α-detection ensures non-susceptibility to chemical exchange with the solvent and enables chemical shift assignment of consecutive proline residues, typically abundant in IDPs. However, many IDPs undergo a disorder-to-order transition upon interaction with their target protein, which leads to the loss of the favorable relaxation properties. Long coherence transfer routes now result in prohibitively large decrease in sensitivity. We introduce a novel 4D ¹H^α-dete

SUBMITTER: Karjalainen M 

PROVIDER: S-EPMC7701164 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature