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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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  
Old 11-24-2010, 11:14 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 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 can be used with weakly aligned micelle and small bicelle samples. Solid-state NMR methods can be used with mechanically aligned bilayer and magnetically aligned bicelle samples.

PMID: 15808228 [PubMed - indexed for MEDLINE]



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 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
A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field.
A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field. A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field. J Magn Reson. 2011 Jan 21; Authors: Lu GJ, Son WS, Opella SJ A general method for assigning...
nmrlearner Journal club 0 02-15-2011 07:17 PM
A General Assignment Method for Oriented Sample (OS) Solid-state NMR of Proteins Based on The Correlation of Resonances through Heteronuclear Dipolar Couplings in Samples Aligned Parallel and Perpendicular to the Magnetic Field
A General Assignment Method for Oriented Sample (OS) Solid-state NMR of Proteins Based on The Correlation of Resonances through Heteronuclear Dipolar Couplings in Samples Aligned Parallel and Perpendicular to the Magnetic Field Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 21 January 2011</br> George J., Lu , Woo Sung, Son , Stanley J., Opella</br> A general method for assigning oriented sample (OS) solid-state NMR spectra of proteins is demonstrated. In principle, this method requires only a single sample of a...
nmrlearner Journal club 0 01-22-2011 03:52 PM
[NMR paper] High-resolution NMR spectroscopy of membrane proteins in aligned bicelles.
High-resolution NMR spectroscopy of membrane proteins in aligned bicelles. Related Articles High-resolution NMR spectroscopy of membrane proteins in aligned bicelles. J Am Chem Soc. 2004 Dec 1;126(47):15340-1 Authors: De Angelis AA, Nevzorov AA, Park SH, Howell SC, Mrse AA, Opella SJ High-resolution solid-state NMR spectra can be obtained from uniformly (15)N-labeled membrane proteins in magnetically aligned bicelles. Fast uniaxial diffusion about the axis of the bilayer normal results in single-line spectra that contain the orientational...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] Structure determination of aligned samples of membrane proteins by NMR spectroscopy.
Structure determination of aligned samples of membrane proteins by NMR spectroscopy. Related Articles Structure determination of aligned samples of membrane proteins by NMR spectroscopy. Magn Reson Chem. 2004 Feb;42(2):162-71 Authors: Nevzorov AA, Mesleh MF, Opella SJ The paper briefly reviews the process of determining the structures of membrane proteins by NMR spectroscopy of aligned samples, describes the integration of recent developments in the interpretation of spectra of aligned proteins and illustrates the application of these methods...
nmrlearner Journal club 0 11-24-2010 09:25 PM
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...
nmrlearner Journal club 0 10-22-2010 04:33 PM



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 01:40 AM.


Map