NDLI: Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen

Content Provider	Springer Nature Link
Author	Al Abdul Wahid, M. Sameer Verardi, Raffaello Veglia, Gianluigi Prosser, R. Scott
Copyright Year	2011
Abstract	In studies of membrane proteins, knowledge of protein topology can provide useful insight into both structure and function. In this work, we present a solution NMR method for the measurement the tilt angle and average immersion depth of alpha helices in membrane proteins, from analysis of the paramagnetic relaxation rate enhancements arising from dissolved oxygen. No modification to the micelle or protein is necessary, and the topology of both transmembrane and amphipathic helices are readily determined. We apply this method to the measure the topology of a monomeric mutant of phospholamban (AFA-PLN), a 52-residue membrane protein containing both an amphipathic and a transmembrane alpha helix. In dodecylphosphocholine micelles, the amphipathic helix of AFA-PLN was found to have a tilt angle of 87° ± 1° and an average immersion depth of 13.2 Å. The transmembrane helix was found to have an average immersion depth of 5.4 Å, indicating residues 41 and 42 are closest to the micelle centre. The resolution of paramagnetic relaxation rate enhancements from dissolved oxygen compares favourably to those from Ni (II), a hydrophilic paramagnetic species.
Starting Page	173
Ending Page	183
Page Count	11
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	51
Issue Number	1-2
e-ISSN	15735001
Language	English
Publisher	Springer Netherlands
Publisher Date	2011-09-27
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Membrane protein immersion depth Membrane protein topology Paramagnetic relaxation rate enhancements Solution state NMR of membrane proteins Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

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