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 08-22-2010, 02:27 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,583
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 Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and s

Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and suppression of decoupling sidebands.

Related Articles Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and suppression of decoupling sidebands.

J Magn Reson B. 1996 Feb;110(2):219-24

Authors: Weigelt J, Hammarstroem A, Bermel W, Otting G



PMID: 8819765 [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
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy Abstract Relaxation violated coherence transfer NMR spectroscopy (Tugarinov et al. in J Am Chem Soc 129:1743â??1750, 2007) is an established experimental tool for quantitative estimation of the amplitudes of side-chain motions in methyl-protonated, highly deuterated proteins. Relaxation violated coherence transfer experiments monitor the build-up of methyl proton multiple-quantum coherences that can be created in magnetically equivalent...
nmrlearner Journal club 0 02-11-2012 10:31 AM
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra Abstract Here we describe phasing anomalies observed in gradient sensitivity enhanced 15N-1H HSQC spectra, and analyze their origin. It is shown that, as a result of 15N off-resonance effects, dispersive contributions to the 1H signal become detectable, and lead to 15N-offset dependent phase errors. Strategies that effectively suppress these artifacts are presented. Content Type Journal Article Category Article Pages 199-207
nmrlearner Journal club 0 09-30-2011 08:01 PM
[Question from NMRWiki Q&A forum] adiabatic decoupling
adiabatic decoupling Hi NMRwikiers, for measuring scalar couplings we use some HSQC pulse sequences modified for obtaining the coupling in F1-dimension as a splitting of doublets for CH2 groups. As high resolution is needed we use high folding in the acqusition, but as a result we obtain a lot of coupling artifacts in phenyl signals. We think that the use of adiabatic decoupling schemes should give a reasonably good spectrum of phenyls but I have no experience in adiabatic decoupling. Anyone can give me a hand for Bruker spectrometers? Check if somebody has answered this question on...
nmrlearner News from other NMR forums 0 05-24-2011 10:02 PM
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra. Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra. J Magn Reson. 2011 Mar 6; Authors: De Sanctis S, Malloni WM, Kremer W, Tomé AM, Lang EW, Neidig KP, Kalbitzer HR NMR spectroscopy in biology and medicine is generally performed in aqueous solutions, thus in (1)H NMR spectroscopy, the dominant signal often stems from the partly suppressed solvent and can be many orders of...
nmrlearner Journal club 0 04-05-2011 10:22 PM
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 February 2011</br> Monika, Bayrhuber , Roland, Riek</br> Sensitivity enhancement in liquid state nuclear magnetic resonance (NMR) triple resonance experiments for the sequential assignment of proteins is important for the investigation of large proteins or protein complexes. We present here the 3D TROSY-MQ/CRINEPT-HN(CO)CA which makes...
nmrlearner Journal club 0 02-04-2011 07:03 AM
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy. A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy. Anal Bioanal Chem. 2011 Jan 11; Authors: Tsiafoulis CG, Exarchou V, Tziova PP, Bairaktari E, Gerothanassis IP, Troganis AN The rapid and accurate determination of specific metabolites present in biofluids is a very demanding task which is essential...
nmrlearner Journal club 0 01-12-2011 11:11 AM
[Question from NMRWiki Q&A forum] How does removal and re-installation of probe affect shims?
How does removal and re-installation of probe affect shims? If you remove and later (not too much later) reinstall the probe and you are confident that probe position inside the magnet does not change at all - would you expect the shim set to change? Do eddy currents due to probe movement affect field homogeneity? Thanks.
nmrlearner News from other NMR forums 0 08-22-2010 02:30 AM
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies Jakob J. Lopez, Christoph Kaiser, Sarika Shastri and Clemens Glaubitz Journal of Biomolecular NMR; 2008; 41(2) pp 97 - 104 Abstract: 13C homonuclear correlation spectra based on proton driven spin diffusion (PDSD) are becoming increasingly important for obtaining distance constraints from multiply labeled biomolecules by MAS NMR. One particular challenging situation arises when such constraints are to be obtained from spectra with a large natural abundance signal background which...
linawaed Journal club 0 08-04-2008 04:01 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 - 2017, 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 05:18 PM.


Map