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 10-22-2010, 04:33 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,613
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 Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi

Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.

Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.

J Phys Chem B. 2010 Oct 20;

Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ

The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large effect on both their structure and dynamics. Reproducing this environment in samples suitable for spectroscopic and diffraction experiments is a key issue, and flexibility in sample preparation is essential to accommodate the diverse size, shape, and other physical properties of membrane proteins. In most cases, to ensure that the biological activities are maintained, this means reconstituting the proteins in fully hydrated planar phospholipid bilayers. The asymmetric character of protein-containing bilayers means that it is possible to prepare either oriented or unoriented (powder) samples. Here we demonstrate the equivalence of mechanical, magnetic, and what we refer to as "rotational alignment" of membrane proteins in phospholipid bilayer samples for solid-state NMR spectroscopy. The trans-membrane domain of virus protein "u" (Vpu) from human immunodeficiency virus (HIV-1) and the full-length membrane-bound form of fd bacteriophage coat protein in phospholipid bilayers are used as examples. The equivalence of structural constraints from oriented and unoriented (powder) samples of membrane proteins is based on two concepts: (1) their alignment is defined by the direction of the bilayer normal relative to the magnetic field and (2) they undergo rapid rotational diffusion about the same bilayer normal in liquid crystalline membranes. The measurement of angular constraints relative to a common external axis system defined by the bilayer normal for all sites in the protein is an essential element of oriented sample (OS) solid-state NMR.

PMID: 20961141 [PubMed - as supplied by publisher]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
nmrlearner Journal club 0 10-10-2011 06:27 AM
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: Sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles.
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: Sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles. Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: Sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles. J Magn Reson. 2011 Jul 2; Authors: Tang W, Nevzorov AA Thermodynamic limit of magnetization corresponding to the intact proton bath usually cannot be transferred...
nmrlearner Journal club 0 07-26-2011 09:30 PM
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 2 July 2011</br> Wenxing, Tang , Alexander A., Nevzorov</br> Thermodynamic limit of magnetization corresponding to the intact proton bath often cannot be transferred in a single cross-polarization contact. This is mainly due to the finite ratio between the number densities of the high-...
nmrlearner Journal club 0 07-05-2011 05:52 AM
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers. Related Articles Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers. J Am Chem Soc. 2010 Dec 2; Authors: Kupc?e E, Kay LE, Freeman R We show that the weak signal that remains after (13)C-detected experiments (the (13)C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA(CO)NNH, into a single pulse sequence that makes use of two receivers...
nmrlearner Journal club 0 12-04-2010 07:24 PM
[NMR tweet] How is "Tyrannosaurus" related to "Nuclear Magnetic Resonance"? http://www.threewiki.com/60YeHE @threewiki
How is "Tyrannosaurus" related to "Nuclear Magnetic Resonance"? http://www.threewiki.com/60YeHE @threewiki Published by Jakob7 (Jakob Baumhardt) on 2010-12-04T05:24:13Z Source: Twitter
nmrlearner Twitter NMR 0 12-04-2010 05:30 AM
[NMR paper] NMR experiments on aligned samples of membrane proteins.
NMR experiments on aligned samples of membrane proteins. Related Articles NMR experiments on aligned samples of membrane proteins. Methods Enzymol. 2005;394:350-82 Authors: De Angelis AA, Jones DH, Grant CV, Park SH, Mesleh MF, Opella SJ NMR methods can be used to determine the structures of membrane proteins. Lipids can be chosen so that protein-containing micelles, bicelles, or bilayers are available as samples. All three types of samples can be aligned weakly or strongly, depending on their rotational correlation time. Solution NMR methods...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein
Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. Related Articles Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. J Magn Reson. 2000 Oct;146(2):381-4 Authors: Ma C, Opella SJ Twelve amino acid residues corresponding to an "EF-hand" calcium-binding site were added to the N-terminus of a protein, providing a specific lanthanide ion binding that weakly orients the protein in solution. A...
nmrlearner Journal club 0 11-19-2010 08:29 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 - 2024, 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 05:49 PM.


Map