Related ArticlesComplexes of photosynthetic redox proteins studied by NMR.
Photosynth Res. 2004;81(3):277-87
Authors: Ubbink M
In the photosynthetic redox chain, small electron transfer proteins shuttle electrons between the large membrane-associated redox complexes. Short-lived but specific protein:protein complexes are formed to enable fast electron transfer. Recent nuclear magnetic resonance (NMR) studies have elucidated the binding sites on plastocyanin, cytochrome c (6) and ferredoxin. Also the orientation of plastocyanin in complex with cytochrome f has been determined. Based on these results, general features that enable the formation of such transient complexes are discussed.
PMID: 16034532 [PubMed - as supplied by publisher]
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Photosynth Res. 2011 Aug 13;
Authors: Pandit A, de Groot HJ
This short review describes how solid-state NMR has provided a mechanistic and electronic picture of pigment-protein and pigment-pigment interactions in photosynthetic antenna complexes. NMR results on purple bacterial antenna complexes show how the packing of the protein and the pigments inside the light-harvesting oligomers induces mutual...
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[NMR paper] Transient complexes of redox proteins: structural and dynamic details from NMR studie
Transient complexes of redox proteins: structural and dynamic details from NMR studies.
Related Articles Transient complexes of redox proteins: structural and dynamic details from NMR studies.
J Mol Recognit. 2004 Nov-Dec;17(6):524-39
Authors: Prudêncio M, Ubbink M
Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein-protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two-dimensional NMR spectroscopy has been applied to many redox protein...
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[NMR paper] NMR structure determination of proteins and protein complexes larger than 20 kDa.
NMR structure determination of proteins and protein complexes larger than 20 kDa.
Related Articles NMR structure determination of proteins and protein complexes larger than 20 kDa.
Curr Opin Chem Biol. 1998 Oct;2(5):564-70
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional nuclear magnetic resonance methodology to obtain 1H, 15N and 13C resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long-range order, coupled with new methods of structure refinement and novel methods...
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[NMR paper] NMR structures of proteins and protein complexes beyond 20,000 M(r).
NMR structures of proteins and protein complexes beyond 20,000 M(r).
Related Articles NMR structures of proteins and protein complexes beyond 20,000 M(r).
Nat Struct Biol. 1997 Oct;4 Suppl:849-53
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.
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[NMR paper] Protein complexes studied by NMR spectroscopy.
Protein complexes studied by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein complexes studied by NMR spectroscopy.
Curr Opin Biotechnol. 1996 Aug;7(4):403-8
Authors: Wand AJ, Englander SW
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point...
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[NMR paper] Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by N
Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Related Articles Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Biochemistry. 1995 Jan 10;34(1):148-54
Authors: Davis KG, Plyte SE, Robertson SR, Cooper A, Kneale GG
The Pf1 gene 5 protein forms a large helical nucleoprotein complex (Mr = 3.1 x 10(7)) with single-stranded viral DNA, from which a 32 amino acid...
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[NMR paper] Conformational differences between complexes of elongation factor Tu studied 19F-NMR
Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
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 Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
Eur J Biochem. 1993 Dec 15;218(3):1041-7
Authors: Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J
An analogue of elongation factor Tu (EF-Tu) from Escherichia coli was prepared by...
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[NMR paper] Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation
Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.
Arch Biochem Biophys. 1993 Mar;301(2):244-50
Authors: Desideri A, Polticelli F, Falconi M, Sette M, Ciriolo MR, Paci M,...
Complexes of photosynthetic redox proteins studied by NMR.
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