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 04-28-2015, 12:40 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 19,922
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 Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles

Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles

Publication date: Available online 28 April 2015
Source:Journal of Magnetic Resonance

Author(s): Sophie N. Koroloff , Alexander A. Nevzorov

Solid-state NMR (ssNMR) of oriented membrane proteins (MPs) is capable of providing structural and dynamic information at nearly physiological conditions. However, NMR experiments performed on oriented membrane proteins generally suffer from low sensitivity. Moreover, utilization of high-power radiofrequency (RF) irradiations for magnetization transfer may give rise to sample heating, thereby decreasing the efficiency of conventional cross-polarization schemes. Here we have optimized the recently developed Repetitive Cross-Polarization (REP-CP) sequence (Tang et al., JMR 2011) to further increase the magnetization transfer efficiency for membrane proteins reconstituted in magnetically aligned bicelles and compared its performance to single-contact Hartmann-Hahn Cross-Polarization (CP), CP-MOIST and the adiabatic transfer. It has been found that employing the REP-CP sequence at RF-field amplitudes of 19 kHz instead of the commonly used higher RF fields (>45 kHz) enhances the efficiency of REP-CP. An additional 30% signal enhancement can be obtained as compared to the previously published REP-CP, and 20% when compared to the re-optimized REP-CP at 50 kHz RF fields. Moreover, the 15N signal gain of low-power REP-CP was found to be 40% over the adiabatic CP and up to 80% over CP-MOIST. Thus, the low-power REP-CP sequence surpasses all of the previous CP schemes in addition of having the tremendous advantage of reducing the RF powers by a factor of seven, thereby preserving the liquid-like bicelle sample. By contrast, in purely static (NAL crystal) and semi-rigid systems (Pf1 phage), the adiabatic CP was found to be more effective. Periodic intensity oscillations (distinct from the transient oscillations) as a function of the CP contact time and B1 RF field strengths were observed during the REP-CP optimization with the oscillations becoming more pronounced with lower RF fields. Many-spin simulations were performed to explain the oscillations and their periodicity.
Graphical abstract








More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins
From The DNP-NMR Blog: Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins Tesch, D.M. and A.A. Nevzorov, Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins. J Magn Reson, 2014. 239(0): p. 9-15. http://www.ncbi.nlm.nih.gov/pubmed/24355622
nmrlearner News from NMR blogs 0 03-13-2014 05:01 AM
Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins
From The DNP-NMR Blog: Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins Tesch, D.M. and A.A. Nevzorov, Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins. J Magn Reson, 2013. 239C(0): p. 9-15. http://www.ncbi.nlm.nih.gov/pubmed/24355622
nmrlearner News from NMR blogs 0 02-03-2014 03:55 PM
[NMR paper] Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins.
Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins. Related Articles Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins. J Magn Reson. 2013 Nov 28;239C:9-15 Authors: Tesch DM, Nevzorov AA Abstract Elucidating structure and topology of membrane proteins (MPs) is essential for unveiling functionality of these important biological constituents. Oriented-sample...
nmrlearner Journal club 0 12-21-2013 03:15 PM
[NMR paper] Sensitivity Enhancement and Contrasting Information Provided by Free Radicals in Oriented-Sample NMR of Bicelle-Reconstituted Membrane Proteins
Sensitivity Enhancement and Contrasting Information Provided by Free Radicals in Oriented-Sample NMR of Bicelle-Reconstituted Membrane Proteins Publication date: Available online 28 November 2013 Source:Journal of Magnetic Resonance</br> Author(s): Deanna M. Tesch , Alexander A. Nevzorov</br> Elucidating structure and topology of membrane proteins (MPs) is essential for unveiling functionality of these important biological constituents.Oriented-sample solid-state NMR (OS-NMR) is capable of providing such information on MPs under nearly physiological...
nmrlearner Journal club 0 11-28-2013 05:18 PM
A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles
A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles Abstract Oriented-sample NMR (OS-NMR) has emerged as a powerful tool for the structure determination of membrane proteins in their physiological environments. However, the traditional spectroscopic assignment method in OS NMR that uses the ‚??shotgun‚?? approach, though effective, is quite labor- and time-consuming as it is based on the preparation of multiple selectively labeled samples. Here we demonstrate that, by using a combination of the spin exchange under mismatched...
nmrlearner Journal club 0 09-17-2012 02:05 AM
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


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 12:30 PM.


Map