NMR paper NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas

		BioNMR > Educational resources > Journal club
[NMR paper] NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-17-2010, 11:15 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas

NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.

Related Articles NMR spectroscopic studies of the hydrogenosomal [2Fe-2S] ferredoxin from Trichomonas vaginalis: hyperfine-shifted 1H resonances.

J Inorg Biochem. 1998 Dec;72(3-4):127-31

Authors: Liu HY, Germanas JP

The hyperfine-shifted 1H NMR resonances of oxidized and reduced Trichomonas vaginalis ferredoxin, a functionally unique [2Fe-2S] ferredoxin, have been studied. The oxidized protein spectrum displayed a pattern of six broad upfield-shifted resonances between 13 and 40 ppm with chemical shifts distinct from those of other [2Fe-2S] ferredoxins. All hyperfine 1H resonances of the oxidized ferredoxin displayed anti-Curie temperature dependences. Reduced T. vaginalis ferredoxin displayed hyperfine resonances both upfield and downfield of the diamagnetic region. These resonances showed Curie temperature dependences. Overall the hyperfine-shifted NMR spectrum of T. vaginalis ferredoxin, along with other spectroscopic properties, suggested different structural properties for the active center of oxidized hydrogenosomal ferredoxins from those of other [2Fe-2S] ferredoxins.

PMID: 10065531 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking. Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking. Related Articles Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking. FEBS Lett. 2005 Aug 29;579(21):4585-90 Authors: Palma PN, Lagoutte B, Krippahl L, Moura JJ, Guerlesquin F Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
[NMR paper] X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillu X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion. Related Articles X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion. Biochemistry. 2003 Mar 4;42(8):2467-74 Authors: Banci L, Bertini I, Del Conte R, Mangani S, Meyer-Klaucke W XAS studies have been performed, under various experimental conditions, on a copper(I)-transporting protein, CopZ, of Bacillus subtilis....	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fra Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219). Related Articles Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219). Mutat Res. 2001 Jun 5;486(1):1-10 Authors: Buchko GW, Isern NG, Spicer LD, Kennedy MA XPA is a central protein component of nucleotide excision repair (NER), a ubiquitous,...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] NMR spectroscopic studies of I = 1/2 metal ions in biological systems. NMR spectroscopic studies of I = 1/2 metal ions in biological systems. Related Articles NMR spectroscopic studies of I = 1/2 metal ions in biological systems. Biochem Cell Biol. 1998;76(2-3):223-34 Authors: Oz G, Pountney DL, Armitage IM This article reviews the use of nuclear magnetic resonance methods of spin 1/2 metal nuclei to probe the metal binding site(s) in a variety of metalloproteins. The majority of the studies have involved native Zn(II) and Ca(II) metalloproteins where there has been isostructural substitution of these metal ions...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domai MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain. Related Articles MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain. Biochim Biophys Acta. 1995 Dec 6;1253(2):215-23 Authors: Cox MC, Le Brun N, Thomson AJ, Smith A, Morgan WT, Moore GR Heme binding to rabbit hemopexin and its domain I, obtained by proteolytic cleavage of intact hemopexin, was studied by EPR, MCD and 1H-NMR spectroscopies. The data obtained support the proposal that the heme Fe(III) is coordinated by two...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] 1H NMR spectroscopic studies on the interactions between human plasma antithrombin II 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Related Articles 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Biochemistry. 1992 Mar 3;31(8):2286-94 Authors: Horne A, Gettins P The effects of length and composition upon the antithrombin-binding properties of heparin have been investigated for two series of structurally related heparin oligosaccharides. Each...	nmrlearner	Journal club	0	08-21-2010 11:41 PM
[NMR paper] 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum. 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum. Related Articles 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum. Biochem Int. 1992 Mar;26(4):577-85 Authors: Ganadu ML, Bonomi F, Pagani S, Boelens R The 8Fe-8S ferredoxin from Clostridium pasteurianum was investigated by 1D and 2D 1H NMR. Spectra of a well-structured, full native preparation of the oxidized protein in 1 M NaCl at pH 8.0 are presented. Assignments of non-isotropically shifted resonances in the diamagnetic region of the spectrum,...	nmrlearner	Journal club	0	08-21-2010 11:41 PM
[NMR paper] 1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium p 1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianum. 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 studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianum. Eur J Biochem. 1992 Mar 1;204(2):831-9 Authors: Bertini I, Briganti F, Luchinat C, Messori L, Monnanni R, Scozzafava A, Vallini G The ferredoxin from Clostridium pasteurianum, containing two...	nmrlearner	Journal club	0	08-21-2010 11:41 PM

« Previous Thread | Next 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