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 03-14-2014, 06:40 AM
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 High-resolution heteronuclear multi-dimensional NMR spectroscopy in magnetic fields with unknown spatial variations.

High-resolution heteronuclear multi-dimensional NMR spectroscopy in magnetic fields with unknown spatial variations.

Related Articles High-resolution heteronuclear multi-dimensional NMR spectroscopy in magnetic fields with unknown spatial variations.

J Magn Reson. 2014 Feb 20;242C:49-56

Authors: Zhang Z, Huang Y, Smith PE, Wang K, Cai S, Chen Z

Abstract
Heteronuclear NMR spectroscopy is an extremely powerful tool for determining the structures of organic molecules and is of particular significance in the structural analysis of proteins. In order to leverage the method's potential for structural investigations, obtaining high-resolution NMR spectra is essential and this is generally accomplished by using very homogeneous magnetic fields. However, there are several situations where magnetic field distortions and thus line broadening is unavoidable, for example, the samples under investigation may be inherently heterogeneous, and the magnet's homogeneity may be poor. This line broadening can hinder resonance assignment or even render it impossible. We put forth a new class of pulse sequences for obtaining high-resolution heteronuclear spectra in magnetic fields with unknown spatial variations based on distant dipolar field modulations. This strategy's capabilities are demonstrated with the acquisition of high-resolution 2D gHSQC and gHMBC spectra. These sequences' performances are evaluated on the basis of their sensitivities and acquisition efficiencies. Moreover, we show that by encoding and decoding NMR observables spatially, as is done in ultrafast NMR, an extra dimension containing J-coupling information can be obtained without increasing the time necessary to acquire a heteronuclear correlation spectrum. Since the new sequences relax magnetic field homogeneity constraints imposed upon high-resolution NMR, they may be applied in portable NMR sensors and studies of heterogeneous chemical and biological materials.


PMID: 24607822 [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
High-resolution heteronuclear multi-dimensional NMR spectroscopy in magnetic fields with unknown spatial variations
High-resolution heteronuclear multi-dimensional NMR spectroscopy in magnetic fields with unknown spatial variations Publication date: Available online 20 February 2014 Source:Journal of Magnetic Resonance</br> Author(s): Zhiyong Zhang , Yuqing Huang , Pieter E.S. Smith , Kaiyu Wang , Shuhui Cai , Zhong Chen</br> Heteronuclear NMR spectroscopy is an extremely powerful tool for determining the structures of organic molecules and is of particular significance in the structural analysis of proteins. In order to leverage the method’s potential for structural...
nmrlearner Journal club 0 02-20-2014 05:15 AM
[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling. Related Articles Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling. Chem Commun (Camb). 2013 Dec 23; Authors: Helge Meyer N, Zangger K Abstract Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear...
nmrlearner Journal club 0 12-25-2013 03:39 PM
High Resolution Para-Hydrogen Induced Polarization in Inhomogeneous Magnetic Fields
From the The DNP-NMR Blog: High Resolution Para-Hydrogen Induced Polarization in Inhomogeneous Magnetic Fields Buljubasich, L., et al., High Resolution Para-Hydrogen Induced Polarization in Inhomogeneous Magnetic Fields. J. Magn. Reson., 2013(0). http://dx.doi.org/10.1016/j.jmr.2013.02.008
nmrlearner News from NMR blogs 0 04-15-2013 08:52 AM
Achieving high spatial resolution and high SNR in low-field MRI of hyperpolarised gases with Slow Low Angle SHot
From the The DNP-NMR Blog: Achieving high spatial resolution and high SNR in low-field MRI of hyperpolarised gases with Slow Low Angle SHot Safiullin, K., C. Talbot, and P.J. Nacher, Achieving high spatial resolution and high SNR in low-field MRI of hyperpolarised gases with Slow Low Angle SHot. J Magn Reson, 2013. 227(0): p. 72-86. http://dx.doi.org/10.1016/j.jmr.2012.11.025
nmrlearner News from NMR blogs 0 04-15-2013 08:52 AM
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins Abstract Well-resolved 2Hâ??13C correlation spectra, reminiscent of 1Hâ??13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2Hâ??13C transfer step in a reasonable time....
nmrlearner Journal club 0 11-01-2011 01:52 AM
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field Abstract Magic-angle spinning (MAS) solid-state NMR (SSNMR) spectroscopy of uniformly-13C,15N labeled protein samples provides insight into atomic-resolution chemistry and structure. Data collection efficiency has advanced remarkably in the last decade; however, the study of larger proteins is still challenged by relatively low resolution in comparison to solution NMR. In this study, we present a systematic analysis of SSNMR protein spectra acquired at 11.7, 17.6 and 21.1 Tesla (1H frequencies of...
nmrlearner Journal club 0 01-09-2011 12:46 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 05:41 AM.


Map