Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under Magic Angle Spinning

S. Luca, D. V. Filippov, J. H. Van Boom, H. Oschkinat, H. J.M. De Groot, M. Baldus

Research output: Contribution to journalArticlepeer-review

120 Scopus citations

Abstract

Resonance assignments recently obtained on immobilized polypeptides and a membrane protein aggregate under Magic Angle Spinning are compared to random coil values in the liquid state. The resulting chemical shift differences (secondary chemical shifts) are evaluated in light of the backbone torsion angle ψ previously reported using X-ray crystallography. In all cases, a remarkable correlation is found suggesting that the concept of secondary chemical shifts, well established in the liquid state, can be of similar importance in the context of multiple-labelled polypeptides studied under MAS conditions.

Original languageEnglish (US)
Pages (from-to)325-331
Number of pages7
JournalJournal of Biomolecular NMR
Volume20
Issue number4
DOIs
StatePublished - 2001

Keywords

  • Chemical shifts
  • Magic angle spinning
  • Membrane proteins
  • Protein aggregates
  • Secondary structure
  • Solid-state NMR

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

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