Related ArticlesLight-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.
Biophys Chem. 1990 May;36(1):27-31
Authors: Albert AD, Frye JS, Yeagle PL
Magic angle spinning 31P-NMR (MAS 31P-NMR) spectra of bovine rod outer segments, unphosphorylated and phosphorylated, were obtained. In the phosphorylated samples the spectra showed new resonances not assignable to phospholipids. These signals were present only when stimulation of receptor phosphorylation occurred. These resonances were not due to exogenous, soluble phosphorus-containing compounds. Limited proteolysis to remove the carboxyl-terminal region of the photoreceptor that contains the phosphorylation sites removed these resonances. The chemical shifts were in the usual range for serine phosphate and threonine phosphate. The pKa obtained from a pH titration of the 31P chemical shift was typical of serine phosphate. Therefore, these 31P-NMR resonances were assigned to the phosphorylation sites on membrane proteins in the rod outer segment disk membranes. Static 31P-NMR measurements revealed that at least some of these sites gave rise to relatively narrow resonances, indicative of considerable motional freedom of the carboxyl-terminal segment of the photoreceptor when phosphorylated. These data indicate that it is possible to study phosphorylation sites on membrane proteins using MAS 31P-NMR, and that using in vivo 31P 'spin labelling' one can study directly and selectively regions of receptors crucial to receptor function.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
nmrlearner
Journal club
0
03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I
nmrlearner
Journal club
0
03-02-2011 02:01 AM
[NMR paper] Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Related Articles Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Chembiochem. 2005 Sep;6(9):1679-84
Authors: Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H
Uniformly 13C-,15N-labelled outer-membrane protein G (OmpG) from Escherichia coli was expressed for structural studies by solid-state magic-angle spinning (MAS) NMR. Inclusion bodies of the recombinant, labelled protein...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
Related Articles Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
Nat Struct Biol. 2001 Apr;8(4):334-8
Authors: Arora A, Abildgaard F, Bushweller JH, Tamm LK
We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta-barrel...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasm
Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
Related Articles Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
J Mol Biol. 2001 Mar 30;307(3):871-84
Authors: Ramelot TA, Nicholson LK
The cytoplasmic tail of the amyloid precursor protein (APPc) interacts with several cellular factors implicated in intracellular signaling or proteolytic production of amyloid beta peptide found in senile plaques of Alzheimer's disease...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX
Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.
Related Articles Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2358-63
Authors: Fernández C, Adeishvili K, Wüthrich K
The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by
Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.
Protein Sci. 1996...