Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues

DOI

Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein–protein interactions. We studied aromatic residues in the two structurally homologous cross-β amyloid fibrils HET-s, and HELLF by employing a specific isotope-labeling approach and magic-angle-spinning NMR. The dynamic behavior of the aromatic residues Phe and Tyr indicates that the hydrophobic amyloid core is rigid, without any sign of "breathing motions" over hundreds of milliseconds at least. Aromatic residues exposed at the fibril surface have a rigid ring axis but undergo ring flips on a variety of time scales from nanoseconds to microseconds. Our approach provides direct insight into hydrophobic-core motions, enabling a better evaluation of the conformational heterogeneity generated from an NMR structural ensemble of such amyloid cross-β architecture.

Identifier
DOI https://doi.org/10.15479/AT:ISTA:12497
Metadata Access https://research-explorer.app.ist.ac.at/oai?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai:pub.research-explorer.app.ist.ac.at:12497
Provenance
Creator Becker, Lea Marie; Schanda, Paul
Publisher Institute of Science and Technology Austria
Publication Year 2023
Rights https://creativecommons.org/licenses/by-nc/4.0/; info:eu-repo/semantics/openAccess
OpenAccess true
Contact repository.manager(at)ist.ac.at
Representation
Resource Type info:eu-repo/semantics/other; doc-type:ResearchData; Text; http://purl.org/coar/resource_type/c_ddb1
Discipline Life Sciences, Natural Sciences, Engineering Sciences