Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy

Andrew J. Nieuwkoop, Chad M. Rienstra

Research output: Contribution to journalArticle

Abstract

We demonstrate that 3D Z-filtered TEDOR experiments, when performed on mixtures of isotopically labeled protein samples, report on site-specific intermolecular distance restraints. These data sets can be leveraged to perform rigorous structure calculations of the protein interface. In the example demonstrated here, we determine the packing arrangement of our nanocrystalline GB1 preparation to be consistent with the trigonal form as determined by X-ray diffraction. This represents an important proof of principle, in a case where the results can be directly compared with other structural information. We envision the application of this approach to determining the registry and quaternary arrangement of protein fibrils, which most often cannot be determined by diffraction methods.

Original languageEnglish (US)
Pages (from-to)7570-7571
Number of pages2
JournalJournal of the American Chemical Society
Volume132
Issue number22
DOIs
StatePublished - Jun 9 2010

    Fingerprint

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this