BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > NMR Questions and Answers
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 08-10-2006, 10:20 PM
Junior Member
 
Join Date: Aug 2006
Posts: 1
Points: 22, Level: 1
Points: 22, Level: 1 Points: 22, Level: 1 Points: 22, Level: 1
Level up: 43%, 28 Points needed
Level up: 43% Level up: 43% Level up: 43%
Activity: 0%
Activity: 0% Activity: 0% Activity: 0%
NMR Credits: 0
NMR Points: 22
Downloads: 0
Uploads: 0
Default Unanswered:

is dipolar dephasing one of the contributing mechanisms to T2 or they are different ? Thanks
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
NMR Excitation, Dephasing and Spin Echoes
NMR Excitation, Dephasing and Spin Echoes http://i.ytimg.com/vi/KtWnmFg-u5g/default.jpg NMR Excitation, Dephasing and Spin Echoes This short animation shows the process of NMR excitation in the laboratory and the rotating frame, as well as the dephasing that occurs from field inhomogeneity and the formation of the Hahn spin echo. Please credit (c)2010 Mark Cohen (mscohen@ucla.edu) during re-use. From:markcat3t Views:8653 http://gdata.youtube.com/static/images/icn_star_full_11x11.gif http://gdata.youtube.com/static/images/icn_star_full_11x11.gif...
nmrlearner NMR educational videos 0 01-29-2012 07:45 PM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR. The Use of Residual Dipolar Coupling in Studying Proteins by NMR. Top Curr Chem. 2011 Sep 28; Authors: Chen K, Tjandra N Abstract The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
nmrlearner Journal club 0 09-30-2011 05:59 AM
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR. Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR. J Magn Reson. 2011 Mar 17; Authors: Traaseth NJ, Veglia G We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR...
nmrlearner Journal club 0 04-13-2011 11:57 PM
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 March 2011</br> Nathaniel J., Traaseth , Gianluigi, Veglia</br> We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR spectra of membrane proteins in fluid lipid membranes with broad lines and...
nmrlearner Journal club 0 03-18-2011 06:43 AM
[NMR paper] Transverse dephasing optimized solid-state NMR spectroscopy.
Transverse dephasing optimized solid-state NMR spectroscopy. Related Articles Transverse dephasing optimized solid-state NMR spectroscopy. J Am Chem Soc. 2003 Nov 19;125(46):13938-9 Authors: De Paëpe G, Giraud N, Lesage A, Hodgkinson P, Böckmann A, Emsley L It is shown how coherence lifetimes in solid-state NMR experiments can be controlled. New decoupling schemes are introduced which actively optimize dephasing times, providing increases of up to a factor of 2 with respect to the best existing schemes. The new schemes are implemented in...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Dipolar Waves as NMR maps of helices in proteins.
Dipolar Waves as NMR maps of helices in proteins. Related Articles Dipolar Waves as NMR maps of helices in proteins. J Magn Reson. 2003 Aug;163(2):288-99 Authors: Mesleh MF, Opella SJ Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Dipolar waves as NMR maps of protein structure.
Dipolar waves as NMR maps of protein structure. Related Articles Dipolar waves as NMR maps of protein structure. J Am Chem Soc. 2002 Apr 24;124(16):4206-7 Authors: Mesleh MF, Veglia G, DeSilva TM, Marassi FM, Opella SJ The anisotropy of nuclear spin interactions results in a unique mapping of structure to the resonance frequencies and split tings observed in NMR spectra, however, the determination of molecular structure from experimentally measured spectral parameters is complicated by angular ambiguities resulting from the symmetry properties...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[U. of Ottawa NMR Facility Blog] The Dephasing Power of Pulsed Field Gradients
The Dephasing Power of Pulsed Field Gradients Pulsed field gradients are used in many modern NMR measurements to select specific coherence pathways and eliminate (or at least minimize) the need for time consuming pulse and receiver phase cycles. The gradients are most often used in conjunction with spin echos such that unwanted coherences can be dephased and the desired coherences can be rephased. They are also used to measure diffusion constants or collect DOSY data. It is instructive to examine the magnetization vectors in the active volume of an NMR tube as a function of the gradient...
nmrlearner News from NMR blogs 0 08-21-2010 08:15 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 12:54 AM.


Map