Abstract:
:Oriented solid-state NMR in combination with multiple-residue-specific (15)N labeling and extensive numerical spectral analysis is proposed to determine helix conformations of large membrane proteins in native membranes. The method is demonstrated on uniaxially oriented samples of (15)N-methionine, -valine, and -glycine-labeled bacteriorhopsin in native purple membranes. Experimental two-dimensional (1)H-(15)N dipole-dipole coupling versus (15)N chemical shift spectra for all samples are analyzed numerically to establish combined constraints on the orientation of the seven transmembrane helices relative to the membrane bilayer normal. Since the method does not depend on specific resonance assignments and proves robust toward nonidealities in the sample alignment, it may be generally feasible for the study of conformational arrangement and function-induced conformation changes of large integral membrane proteins.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Vosegaard T,Kamihira-Ishijima M,Watts A,Nielsen NCdoi
10.1529/biophysj.107.116004subject
Has Abstractpub_date
2008-01-01 00:00:00pages
241-50issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(08)70783-5journal_volume
94pub_type
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