Related ArticlesStructural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectroscopy study.
Biochemistry. 1990 Dec 18;29(50):11057-67
Authors: Lecomte JT, Cocco MJ
The structural properties of the complex formed by apomyoglobin and protoporphyrin IX (des-iron myoglobin) were studied to probe the influence of iron-to-histidine coordination on the native myoglobin fold and the heme binding site geometry. Standard two-dimensional proton nuclear magnetic resonance spectroscopy methods were applied to identify porphyrin and protein signals. A pronounced spectral resemblance between carbonmonoxymyoglobin and des-iron myoglobin was noticed that could be exploited to assign a number of resonances by nuclear Overhauser spectroscopy. Protoporphyrin IX was determined to bind in the same orientation as the heme. Most residues in contact with the prosthetic group were found in the holomyoglobin conformation. Several tertiary structure features were also characterized near the protein termini. It was concluded that the protoporphyrin-apomyoglobin interactions are capable of organizing the binding site and the unfolded region of the apoprotein into the native holoprotein structure.
[NMR paper] The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H in
The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.
Related Articles The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.
Proteins. 1996 Jul;25(3):267-85
Authors: Lecomte JT, Kao YH, Cocco MJ
Proton nuclear magnetic resonance spectroscopy was applied to sperm whale apomyoglobin to describe the conformation adopted by the protein under native conditions. The study focused on the A-B-G-H...
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[NMR paper] Is apomyoglobin a molten globule? Structural characterization by NMR.
Is apomyoglobin a molten globule? Structural characterization by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Is apomyoglobin a molten globule? Structural characterization by NMR.
J Mol Biol. 1996 Nov 8;263(4):531-8
Authors: Eliezer D, Wright PE
Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural information on isotopically labeled recombinant sperm whale apomyoglobin in the native state at pH 6.1. Assignments for backbone...
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[NMR paper] Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Related Articles Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Biochemistry. 1995 May 16;34(19):6488-503
Authors: Borer PN, Lin Y, Wang S, Roggenbuck MW, Gott JM, Uhlenbeck OC, Pelczer I
The three-dimensional conformation of a 24-nucleotide variant of the RNA binding sequence for the coat protein of bacteriophage R17 has been analyzed using NMR, molecular dynamics, and energy minimization. The imino proton spectrum is consistent with base pairing...
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[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
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[NMR paper] The native state of apomyoglobin described by proton NMR spectroscopy: interaction wi
The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS.
...
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[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
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08-22-2010 03:33 AM
[NMR paper] The native state of apomyoglobin described by proton NMR spectroscopy: interaction wi
The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS.
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[NMR paper] Some structural features of cluster-coordinating cysteines of Clostridium pasteurianu
Some structural features of cluster-coordinating cysteines of Clostridium pasteurianum ferredoxin are revealed by 2D TOCSY 1H NMR on the oxidized protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Some structural features of cluster-coordinating cysteines of Clostridium pasteurianum ferredoxin are revealed by 2D TOCSY 1H NMR on the oxidized protein.
Biochem Biophys Res Commun. 1994 Jul 15;202(1):591-5
Authors: Acquotti D, Bonomi F, Brocca P, Ganadu ML, Pagani S
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Structural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectros
Linear Mode
