Nuclear Magnetic Resonance Characterization of the Myristoylated, N-Terminal Fragment of ADP-Ribosylation Factor 1 in a Magnetically Oriented Membrane Array
- 1 January 1998
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 37 (2) , 706-716
- https://doi.org/10.1021/bi9717791
Abstract
The behavior of the N-terminal fragment of human ADP-ribosylation factor 1 (ARF1) in a membranelike environment is described. This is accomplished using heteronuclear liquid crystal NMR techniques in a magnetically oriented membrane array on a selectively 13C- and 15N-labeled peptide. After full assignment of the labeled sites, residual dipolar couplings (13C-13C, 15N-1H and, 13C-15N) and chemical shift anisotropy effects (amide 13C and 15N) were measured. The experimental data were interpreted using order matrix calculations to yield orientational and dynamic information for four separate, rigid amide planes. The experimental data obtained proves that the amphipathic peptide interacts with the bilayer in a mode that is consistent with an alpha-helix having its axis parallel to the membrane surface. Possibilities of extending the employed techniques to larger and uniformly labeled systems are discussed.Keywords
This publication has 11 references indexed in Scilit:
- Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteinsJournal of Biomolecular NMR, 1996
- High-Resolution Solid-State NMR Spectra of Integral Membrane Proteins Reconstituted into Magnetically Oriented Phospholipid BilayersJournal of Magnetic Resonance, Series B, 1996
- Myristoylation-facilitated Binding of the G Protein ARF1GDP to Membrane Phospholipids Is Required for Its Activation by a Soluble Nucleotide Exchange FactorJournal of Biological Chemistry, 1996
- Magnetically Aligned Membrane Model Systems with Positive Order Parameter: Switching the Sign of Szz with Paramagnetic IonsJournal of the American Chemical Society, 1996
- Membrane interaction of small N-myristoylated peptides: implications for membrane anchoring and protein-protein associationBiophysical Journal, 1994
- Facile Acquisition and Assignment of Oriented Sample NMR Spectra for Bilayer Surface-Associated ProteinsJournal of the American Chemical Society, 1994
- NMR cross polarization by adiabatic passage through the Hartmann—Hahn condition (APHH)Chemical Physics Letters, 1994
- Headgroup orientations of alkyl glycosides at a lipid bilayer interfaceJournal of the American Chemical Society, 1992
- Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acidsInternational Journal of Peptide and Protein Research, 1990
- Recent Results in the Field of Liquid CrystalsAngewandte Chemie International Edition in English, 1968