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

Go Back   BioNMR > NMR community > News from other NMR forums
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 06-03-2011, 12:11 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 paramagnetic oxygen in solution NMR

paramagnetic oxygen in solution NMR

A student is running a kinetics experiment in a J-Young tube under 5-10 atm of oxygen, much like in this journal article:http://pubs.acs.org/doi/abs/10.1021/ja9061932
  1. Student is seeing reduction in signal from his compound (slightly polar) and his internal standard (non-polar). Obviously paramagnetic oxygen?
  2. The part I can't figure out: student is NOT seeing a reduction in his solvent peak. Solvent is benzene or toluene. I am assuming he is using at least some deuterated solvent.
I have found a lot of literature on the interaction of paramagnetic O2 with membrane proteins, etc., but the paper the student sent to me makes no mention of accounting for this in the kinetics calculations. Assuming the relaxation of his compound and the internal standard are affected similarly by the paramagnetic O2, the relative integration should be correct? Is the relaxation of the solvent just too long to be affected much by paramagnetic O2? The issue with the kinetics runs is that they typically do one scan per time point since the reaction occurs somewhat quickly and they do not want to average over several scans. If the relaxation is short enough can we just do several scans with very short delay times?



Check if somebody has answered this question on NMRWiki QA forum
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen
Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen Abstract In studies of membrane proteins, knowledge of protein topology can provide useful insight into both structure and function. In this work, we present a solution NMR method for the measurement the tilt angle and average immersion depth of alpha helices in membrane proteins, from analysis of the paramagnetic relaxation rate enhancements arising from dissolved oxygen. No modification to the micelle or protein is necessary, and the topology of both transmembrane and...
nmrlearner Journal club 0 09-30-2011 08:01 PM
In vivo oxygen-17 NMR for imaging brain oxygen metabolism at high field
In vivo oxygen-17 NMR for imaging brain oxygen metabolism at high field Publication year: 2011 Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 23 April 2011</br> Xiao-Hong, Zhu , Wei, Chen</br> *Highlights:*? This article reviews the developments of in vivo 17O NMR imaging in brain research. ? In vivo 17O NMR imaging has improved significantly at high/ultrahigh field. ? In vivo 17O NMR can noninvasively image brain oxygen metabolism and perfusion. ? In vivo 17O NMR is useful for mapping the functional change in oxygen...
nmrlearner Journal club 0 04-24-2011 03:42 PM
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. J Inorg Biochem. 2010 Oct;104(10):1063-70 Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
nmrlearner Journal club 0 02-10-2011 03:51 PM
Elevating Oxygen
Elevating Oxygen Spectroscopy: Technique yields unprecedented resolution in 17O NMR spectra of proteins in solution More...
nmrlearner General 0 01-04-2011 11:03 PM
[NMR paper] Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis
Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy. Related Articles Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy. J Am Chem Soc. 2002 Feb 27;124(8):1778-81 Authors: Luchette PA, Prosser RS, Sanders CR Oxygen solubility increases toward the hydrophobic interior of membranes. Using NMR, this O(2) solubility gradient gives rise to an exquisite range of position-dependent paramagnetic effects at partial pressures of 100...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic p
PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins. Related Articles PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins. J Magn Reson. 1998 Sep;134(1):154-7 Authors: Bondon A, Mouro C A new method for NMR spectra acquisition of paramagnetic proteins is described, based on the simple use of homonuclear broadband decoupling of the diamagnetic region. Several advantages are associated with this method which was applied to one-dimensional spectra, to 1D...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Determination of solution structures of paramagnetic proteins by NMR.
Determination of solution structures of paramagnetic proteins by NMR. Related Articles Determination of solution structures of paramagnetic proteins by NMR. Eur Biophys J. 1998;27(4):367-75 Authors: Turner DL, Brennan L, Chamberlin SG, Louro RO, Xavier AV Standard procedures for using nuclear Overhauser enhancements (NOE) between protons to generate structures for diamagnetic proteins in solution from NMR data may be supplemented by using dipolar shifts if the protein is paramagnetic. This is advantageous since the electron -nuclear dipolar...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin
Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR. Biochemistry. 1997 Sep 30;36(39):11605-18 Authors: Bentrop D, Bertini I, Cremonini MA, Forsén S, Luchinat C, Malmendal A The solution structure of the dicerium(III) complex of the N-terminal domain of calmodulin...
nmrlearner Journal club 0 08-22-2010 05:08 PM


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 - 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 06:49 AM.


Map