Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR

O. C. Andronesi, J. R. Pfeifer, L. Al-Momani, S. Özdirekcan, D. T.S. Rijkers, B. Angerstein, S. Luca, U. Koert, J. A. Killian, M. Baldus

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides under Magic Angle Spinning. The functional dependence of a series of anisotropic recoupling schemes is analyzed using theoretical and numerical methods. These studies lead to the construction of a set of polarization dephasing or transfer units that probe local backbone conformation and overall molecular orientation within the same NMR experiment. Experimental results are shown for a randomly oriented peptide and for two model membrane peptides reconstituted into lipid bilayers and oriented on polymer films according to a method proposed by Bechinger et al.

Original languageEnglish (US)
Pages (from-to)253-265
Number of pages13
JournalJournal of Biomolecular NMR
Volume30
Issue number3
DOIs
StatePublished - Nov 2004
Externally publishedYes

Keywords

  • MAS
  • Membrane proteins
  • NMR
  • Solid-state
  • Structure determination

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

Fingerprint Dive into the research topics of 'Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR'. Together they form a unique fingerprint.

  • Cite this

    Andronesi, O. C., Pfeifer, J. R., Al-Momani, L., Özdirekcan, S., Rijkers, D. T. S., Angerstein, B., Luca, S., Koert, U., Killian, J. A., & Baldus, M. (2004). Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR. Journal of Biomolecular NMR, 30(3), 253-265. https://doi.org/10.1007/s10858-004-3452-3