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 08-21-2010, 10:48 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,615
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 Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with i

Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid.

Related Articles Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid.

Eur J Biochem. 1990 Apr 30;189(2):351-62

Authors: Veitch NC, Williams RJ

The binding of aromatic donor molecules to plant peroxidases has been investigated by examining the complex formed between horseradish peroxidase isoenzyme C and indole-3-propionic acid using two-dimensional 1H-NMR spectroscopy. Despite the relatively high molecular mass and paramagnetism of the protein, this technique can be successfully applied to provide new information on the structure of the complex. A number of relatively well-resolved resonances in certain regions of the one-dimensional spectrum are assigned to amino acid type on the basis of the two-dimensional experiments. Two phenylalanine side chains are found to interact at positions close to the haem group as shown by nuclear Overhauser effect spectroscopy (NOESY). Furthermore, the NOESY spectrum of the complex reveals distinct interactions between these phenylalanine residues and the indole ring of the donor molecule. The binding site is found to comprise of these phenylalanine side chains and also the methyl group of a leucine or valine residue. On the basis of the model structure of horseradish peroxidase isoenzyme C proposed by Welinder and Nørskov-Lauritsen and information from previous studies of the related turnip peroxidases, possible locations for this binding site are discussed. The NMR methods adopted here may be generally applicable to the study of peroxidase--aromatic-donor interactions.

PMID: 2338080 [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
Interaction of epothilone B (patupilone) with microtubules as detected by two-dimensional solid-state NMR spectroscopy.
Interaction of epothilone B (patupilone) with microtubules as detected by two-dimensional solid-state NMR spectroscopy. Interaction of epothilone B (patupilone) with microtubules as detected by two-dimensional solid-state NMR spectroscopy. Angew Chem Int Ed Engl. 2010 Oct 4;49(41):7504-7 Authors: Kumar A, Heise H, Blommers MJ, Krastel P, Schmitt E, Petersen F, Jeganathan S, Mandelkow EM, Carlomagno T, Griesinger C, Baldus M
nmrlearner Journal club 0 03-13-2011 04:01 AM
[NMR paper] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy. Related Articles Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy. Biochemistry. 2001 Jun 19;40(24):7069-76 Authors: Worrall JA, Kolczak U, Canters GW, Ubbink M The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme
Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme C mutants with alanine replacing either Phe142 or Phe143. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme C mutants with alanine replacing either Phe142 or Phe143. Eur J Biochem. 1995 Oct 15;233(2):650-8 Authors: Veitch NC, Williams RJ, Bone NM, Burke JF, Smith AT ...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Related Articles Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy. Biochemistry. 1994 Oct 11;33(40):12032-41 Authors: Yi Q, Erman JE, Satterlee JD Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...
nmrlearner Journal club 0 08-22-2010 03:29 AM
[NMR paper] Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the
Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys. Eur J Biochem. 1992 Jul...
nmrlearner Journal club 0 08-21-2010 11:45 PM
[NMR paper] 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase.
2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase. Related Articles 2D NMR of paramagnetic metalloenzymes: cyanide-inhibited horseradish peroxidase. J Biomol NMR. 1991 Jul;1(2):175-90 Authors: de Ropp JS, Yu LP, La Mar GN Two-dimensional (2D) proton NMR correlation spectroscopy, COSY, and nuclear Overhauser spectroscopy, NOESY, have been used to explore the applicability of these methods for the moderately large (42 KDa), paramagnetic cyanide-inhibited derivative of horseradish peroxidase, HRP-CN. The target...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] 13C and 15N NMR studies on the interaction between 6,7-dimethyl-8-ribityllumazine and
13C and 15N NMR studies on the interaction between 6,7-dimethyl-8-ribityllumazine and lumazine protein. Related Articles 13C and 15N NMR studies on the interaction between 6,7-dimethyl-8-ribityllumazine and lumazine protein. Biochemistry. 1990 Feb 20;29(7):1823-8 Authors: Vervoort J, O'Kane DJ, Müller F, Bacher A, Strobl G, Lee J The interaction between the prosthetic group 6,7-dimethyl-8-(1'-D-ribityl)lumazine and the lumazine apoproteins from two marine bioluminescent bacteria, one from a relatively thermophilic species, Photobacterium...
nmrlearner Journal club 0 08-21-2010 10:48 PM
[NMR paper] The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study.
The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study. Related Articles The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study. Spectrochim Acta A Mol Biomol Spectrosc. 1999 Feb;55A(2):415-20 Authors: Banci L, Pierattelli R The interaction of the nitrate anion with cytochrome c peroxidase has been demonstrated by using 15N-NMR spectroscopy. The results indicate that the nitrate anion binds to the protein in a specific binding site and are consistent with the hypothesis of an interaction...
nmrlearner Journal club 0 08-21-2010 04:03 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 05:05 AM.


Map