Related ArticlesIdentification 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 performed in order to study the dynamic behavior of the reduced recombinant high-potential iron-sulfur protein iso I (HiPIP I) from Ectothiorhodospira halophila, in the microsecond to ms time range. Measurements of R1 rho were performed as a function of the effective spinlock magnetic field amplitude by using both on and off-resonance radio frequency irradiation. The two data sets provided consistent results and were fit globally in order to identify possible exchange processes in an external loop of the reduced HiPIP I. The loop consists of residues 43-45 and the correlation time of the exchange process was determined to be 50 +/- 8 microseconds for the backbone nitrogen of Gln 44.
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin
Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Related Articles Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...
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[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...
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[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...
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[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...
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[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...
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[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...
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[NMR paper] 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...
Identification of slow motions in the reduced recombinant high-potential iron sulfur
Linear Mode
