Related ArticlesA solution model of the complex formed by adrenodoxin and adrenodoxin reductase determined by paramagnetic NMR spectroscopy.
Biochemistry. 2010 Aug 17;49(32):6846-55
Authors: Keizers PH, Mersinli B, Reinle W, Donauer J, Hiruma Y, Hannemann F, Overhand M, Bernhardt R, Ubbink M
Lanthanide tags offer the opportunity to retrieve long-range distance information from NMR experiments that can be used to guide protein docking. To determine whether sufficient restraints can be retrieved for proteins with low solubility and availability, Ln tags were applied in the study of the 65 kDa membrane-associated protein complex formed by the electron carrier adrenodoxin and its electron donor, adrenodoxin reductase. The reductase is only monomeric at low concentration, and the paramagnetic iron-sulfur cluster of adrenodoxin broadens many of the resonances of nuclei in the interface. Guided by the paramagnetic restraints obtained using two Ln-tag attachment sites, protein docking yields a cluster of solutions with an rmsd of 3.2 A. The mean structure is close to the crystal structure of the cross-linked complex, with an rmsd of 4.0 A. It is concluded that with the application of Ln tags paramagnetic NMR restraints for structure determination can be retrieved even for difficult, low-concentration protein complexes.
[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...
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[NMR paper] NMR-based binding screen and structural analysis of the complex formed between alpha-
NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
Related Articles NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
J Biol Chem. 2002 Oct 4;277(40):37439-45
Authors: Zeng H, Hawrot E
The alpha18-mer...
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[NMR paper] An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed
An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Related Articles An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Pac Symp Biocomput. 2001;:67-78
Authors: Alexandrescu AT
Acid-denatured cold shock protein A (CspA) self-assembles into polymers with properties typical of amyloid fibrils. In the present work, a quenched hydrogen exchange experiment was used to probe the interactions of CspA fibrils with solvent. Exchange...
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[NMR paper] Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR an
Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR and molecular modeling studies.
Related Articles Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR and molecular modeling studies.
Biochemistry. 1994 May 31;33(21):6394-407
Authors: Palma PN, Moura I, LeGall J, Van Beeumen J, Wampler JE, Moura JJ
Small electron-transfer proteins such as flavodoxin (16 kDa) and the tetraheme cytochrome c3 (13 kDa) have been used to mimic, in vitro, part of the complex electron-transfer chain...
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[NMR paper] Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR an
Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR and molecular modeling studies.
Related Articles Evidence for a ternary complex formed between flavodoxin and cytochrome c3: 1H-NMR and molecular modeling studies.
Biochemistry. 1994 May 31;33(21):6394-407
Authors: Palma PN, Moura I, LeGall J, Van Beeumen J, Wampler JE, Moura JJ
Small electron-transfer proteins such as flavodoxin (16 kDa) and the tetraheme cytochrome c3 (13 kDa) have been used to mimic, in vitro, part of the complex electron-transfer chain...
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[NMR paper] 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with
13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid.
FEBS Lett. 1992 Nov 9;312(2-3):147-51
Authors: Cheung HT, Birdsall B, Feeney J
13C NMR studies of 13C-labelled ligands bound to dihydrofolate reductase provide (DHFR) a powerful means of...
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[NMR paper] The three-dimensional structure of guanine-specific ribonuclease F1 in solution deter
The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry.
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 The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry.
Eur J Biochem. 1992 Aug 15;208(1):41-51
Authors: Nakai T, Yoshikawa W, Nakamura H, Yoshida H
Two-dimensional 1H-NMR...
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[NMR paper] On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase a
On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
Related Articles On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
J Biochem. 1991 Jan;109(1):144-9
Authors: Fujii S, Nonaka Y, Okamoto M, Miura R
The interaction between 2',5'-ADP and NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria was examined by titrating the enzyme with...
A solution model of the complex formed by adrenodoxin and adrenodoxin reductase deter
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