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: 17,586
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 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nucle

1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.

Related Articles 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.

Biochemistry. 1990 Jun 12;29(23):5633-7

Authors: Cowan JA, Sola M

1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to individual residues has been proposed from a computer graphics analysis of the X-ray structure. Tentative assignments of other resonances are discussed.

PMID: 2386791 [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
[NMR paper] Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Iron uptake by ferritin: NMR relaxometry studies at low iron loads. Related Articles Iron uptake by ferritin: NMR relaxometry studies at low iron loads. J Inorg Biochem. 1998 Sep;71(3-4):153-7 Authors: Vymazal J, Brooks RA, Bulte JW, Gordon D, Aisen P Twenty ferritin samples were prepared at pH 6.5 with average loadings of 0-89 Fe atoms per molecule. Nuclear magnetic relaxation times T1 and T2 were measured at 3 degrees C, 23 degrees C, and at 37 degrees C and at field strength from 0.025 to 1.5 T. The field dependence, temperature dependence,...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Identification of slow motions in the reduced recombinant high-potential iron sulfur
Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements. Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements. J Biomol NMR. 1998 Aug;12(2):307-18 Authors: Banci L, Felli IC, Koulougliotis D Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhod
1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans. 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 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans. Eur J Biochem. 1996 Mar 1;236(2):405-11 Authors: Ciurli S, Cremonini MA, Kofod P, Luchinat C Oxidized and reduced forms of high-potential iron-sulfur protein (HiPIP) from the...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Three-dimensional solution structure of the oxidized high potential iron-sulfur prote
Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Related Articles Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Biochemistry. 1995 Aug 8;34(31):9851-8 Authors: Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P The NMR solution structure of...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] The three-dimensional solution structure of the reduced high-potential iron-sulfur pr
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Related Articles The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry. 1995 Jan 10;34(1):206-19 Authors: Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature has been extended up to 85% of the total protein protons. Ninety...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and imped
NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two clusters. Related Articles NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two clusters. Biochemistry. 1995 Jan 10;34(1):194-205 Authors: Huber JG, Gaillard J, Moulis JM The 2 ferredoxin from Chromatium vinosum has been investigated by 1H and 13C nuclear magnetic resonance. 1H NMR sequence-specific assignments have been obtained for a large majority of...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from
1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis. 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 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis. Eur J Biochem. 1993 Feb 15;212(1):69-78 Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M 1H one-dimensional and two-dimensional NMR spectra have been...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxi
Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2 ferredoxin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2 ferredoxin. Biochemistry. 1999 May 11;38(19):6335-45 Authors: Kyritsis P, Kümmerle R, Huber JG, Gaillard J, Guigliarelli B, Popescu C, Münck E, Moulis JM The ferredoxin from Chromatium vinosum (CvFd) exhibits sequence and structure peculiarities. Its two Fe4S4(SCys)4 clusters have unusually...
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 - 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 03:46 PM.


Map