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 11-19-2010, 08:44 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
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 Protein NMR spin trapping with [methyl-13C(3)]-MNP: application to the tyrosyl radica

Protein NMR spin trapping with [methyl-13C(3)]-MNP: application to the tyrosyl radical of equine myoglobin.

Related Articles Protein NMR spin trapping with [methyl-13C(3)]-MNP: application to the tyrosyl radical of equine myoglobin.

Free Radic Biol Med. 2001 Aug 1;31(3):383-90

Authors: Bose-Basu B, DeRose EF, Chen YR, Mason RP, London RE

Direct spin trapping studies of protein radical adducts are limited as a consequence of the long rotational correlation times and consequent broadening of the ESR resonances. It can be difficult to determine both the nature and number of adduct species present. NMR detection of reduced spin adducts represents an alternate approach which, however, is subject to the limitations of lower sensitivity and a limited capability for isolating the resonances arising from the reduced adduct from other chemistry involving the spin trap. In the present study, we have utilized [methyl-13C(3)]-MNP for the detection and analysis of tyrosyl spin adducts formed as a result of exposure of equine myoglobin to hydrogen peroxide. The methyl-13C label allows high detection sensitivity in two dimensions, narrow line widths and most significantly, removal by dialysis of unreacted spin trap as well as any nonprotein derivatives that may form. For equine myoglobin, it is found that adduct formation involves a single residue-Tyr-103 and further that adduct formation occurs at the C-3 carbon of the amino acid. HMQC-NOESY experiments further revealed the proximity of the labeled methyl groups to both the three aromatic tyrosyl protons as well as the aromatic protons of the nearby Phe-106 residue.

PMID: 11461776 [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
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Water proton spin saturation affects measured protein backboneN spin relaxation rates Publication year: 2011 Source: Journal of Magnetic Resonance, Available online 1 October 2011</br> Kang*Chen, Nico*Tjandra</br> Protein backboneN NMR spin relaxation rates are useful in characterizing the protein dynamics and structures. To observe the protein nuclear-spin resonances a pulse sequence has to include a water suppression scheme. There are two commonly employed methods, saturating or dephasing the water spins with pulse field gradients and keeping them unperturbed with flip-back pulses....
nmrlearner Journal club 0 10-02-2011 08:25 AM
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy Abstract Methyl-transverse relaxation optimized spectroscopy is rapidly becoming the preferred NMR technique for probing structure and dynamics of very large proteins up to ~1 MDa in molecular size. Data interpretation, however, necessitates assignment of methyl groups which still presents a very challenging and time-consuming process. Here we demonstrate that, in combination with a known 3D structure, paramagnetic...
nmrlearner Journal club 0 09-26-2011 06:42 AM
Understanding the radical mechanism of lipoxygenases using 31P NMR spin trapping.
Understanding the radical mechanism of lipoxygenases using 31P NMR spin trapping. Understanding the radical mechanism of lipoxygenases using 31P NMR spin trapping. Bioorg Med Chem. 2011 May 1;19(9):3022-8 Authors: Zoia L, Perazzini R, Crestini C, Argyropoulos DS Abstract In this paper, we use our quantitative (31)P NMR spin trapping methods, already developed for simple oxygen- and carbon-centered radicals, to understand the radical intermediates generated by enzymatic systems and more specifically lipoxygenases. Our methodology...
nmrlearner Journal club 0 08-25-2011 04:10 PM
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing. NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing. Biochemistry. 2011 Mar 25; Authors: Paukstelis PJ, Chari N, Lambowitz AM, Hoffman DW The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNATyr and are structure-stabilizing splicing cofactors for group I introns. Studies with the Neurospora...
nmrlearner Journal club 0 03-29-2011 07:04 PM
Continuous-wave EPR at 275 GHz: Application to high-spin Fe3+ systems
Continuous-wave EPR at 275 GHz: Application to high-spin Fe3+ systems Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 11 March 2011</br> G., Mathies , H., Blok , J.A.J.M., Disselhorst , P., Gast , H., van der Meer , ...</br> The 275 GHz electron-paramagnetic-resonance spectrometer we reported on in 2004 has been equipped with a new probe head, which contains a cavity especially designed for operation in continuous-wave mode. The sensitivity and signal stability that is achieved with this new probe head is illustrated...
nmrlearner Journal club 0 03-12-2011 05:21 PM
[NMR paper] Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-
Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-labeled proteins. Related Articles Amino acid-type edited NMR experiments for methyl-methyl distance measurement in 13C-labeled proteins. J Am Chem Soc. 2004 Aug 11;126(31):9584-91 Authors: Van Melckebeke H, Simorre JP, Brutscher B New NMR experiments are presented for the measurement of methyl-methyl distances in (13)C-labeled proteins from a series of amino acid-type separated 2D or 3D NOESY spectra. Hadamard amino acid-type encoding of the proximal methyl...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(L
Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains. Related Articles Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains. Biochemistry. 2001 Aug 14;40(32):9596-604 Authors: Schüler W, Kloiber K, Matt T, Bister K, Konrat R The solution structure of quail CRP2(LIM2) was significantly improved by using an increased number of NOE constraints obtained from a 13C,15N-labeled...
nmrlearner Journal club 0 11-19-2010 08:44 PM
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping
Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping Peter Würtz, Olli Aitio, Maarit Hellman and Perttu Permi Journal of Biomolecular NMR; 2007; 39(2) pp 97 - 105 Abstract: Simultaneous recording of different NMR parameters is an efficient way to reduce the overall experimental time and speed up structural studies of biological macromolecules. This can especially be beneficial in the case of fast NMR-based drug screening applications or for collecting NOE restraints, where prohibitively long data collection...
stewart Journal club 0 08-05-2008 01:41 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 04:55 PM.


Map