BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 10-07-2014, 02:31 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,036
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.

Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.

Related Articles Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.

Angew Chem Int Ed Engl. 2014 Oct 3;

Authors: Kofuku Y, Ueda T, Okude J, Shiraishi Y, Kondo K, Mizumura T, Suzuki S, Shimada I

Abstract
G-protein-coupled receptors (GPCRs) exist in conformational equilibrium between active and inactive states, and the former population determines the efficacy of signaling. However, the conformational equilibrium of GPCRs in lipid bilayers is unknown owing to the low sensitivities of their NMR signals. To increase the signal intensities, a deuteration method was developed for GPCRs expressed in an insect cell/baculovirus expression system. The NMR sensitivities of the methionine methyl resonances from the ?2 -adrenergic receptor (?2 AR) in lipid bilayers of reconstituted high-density lipoprotein (rHDL) increased by approximately 5-fold upon deuteration. NMR analyses revealed that the exchange rates for the conformational equilibrium of ?2 AR in rHDLs were remarkably different from those measured in detergents. The timescales of GPCR signaling, calculated from the exchange rates, are faster than those of receptor tyrosine kinases and thus enable rapid neurotransmission and sensory perception.


PMID: 25284766 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy. Chemistry. 2014 Mar 13; Authors: Schmidt P, Thomas L, Müller P, Scheidt HA, Huster D Abstract
nmrlearner Journal club 0 03-14-2014 07:34 PM
[NMR paper] ?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy. ?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy. Angew Chem Int Ed Engl. 2013 Aug 16; Authors: Horst R, Liu JJ, Stevens RC, Wüthrich K Abstract
nmrlearner Journal club 0 08-21-2013 08:49 PM
[NMR paper] Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy. Langmuir. 2012 Dec 11;28(49):17071-8 Authors: Wang T, Widanapathirana L, Zhao Y, Hong M Abstract Macrocycles made of cholate building blocks were previously found to...
nmrlearner Journal club 0 05-22-2013 04:43 PM
Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR October 2012 Publication year: 2012 Source:Current Opinion in Structural Biology, Volume 22, Issue 5</br> </br> Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation...
nmrlearner Journal club 0 02-03-2013 10:13 AM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR. Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR. J Am Chem Soc. 2011 Mar 14; Authors: Yang J, Aslimovska L, Glaubitz C Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
nmrlearner Journal club 0 03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR Jun Yang, Lubica Aslimovska and Clemens Glaubitz http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif Journal of the American Chemical Society DOI: 10.1021/ja109766n http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw
nmrlearner Journal club 0 03-15-2011 05:56 AM
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation. Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation. Biophys J. 2010 Nov 17;99(10):3282-9 Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
nmrlearner Journal club 0 03-03-2011 12:34 PM
[NMR paper] Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimension
Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin. Related Articles Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin. Biochim Biophys Acta. 2003 Oct 13;1616(2):127-36 Authors: Saitô H, Yamamoto K, Tuzi S, Yamaguchi S We have recorded...
nmrlearner Journal club 0 11-24-2010 09:16 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2020, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 02:33 AM.


Map