NMR paper Light-induced membrane protein phosphorylation in the bovine rod outer segment. A mag

		BioNMR > Educational resources > Journal club
[NMR paper] Light-induced membrane protein phosphorylation in the bovine rod outer segment. A mag

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-21-2010, 10:48 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,174

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Light-induced membrane protein phosphorylation in the bovine rod outer segment. A mag

Light-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.

Related Articles Light-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.

PMID: 2207270 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
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...	nmrlearner	Journal club	0	08-22-2010 02:27 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off