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[NMR images] Features of an NMR spectrum
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Features of an NMR spectrum
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NMR pictures
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12-20-2011 04:09 PM
[NMR paper] Structural features of the epsilon subunit of the Escherichia coli ATP synthase deter
Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.
Related Articles Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.
Nat Struct Biol. 1995 Nov;2(11):961-7
Authors: Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA
The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The epsilon...
nmrlearner
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08-22-2010 03:50 AM
[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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08-22-2010 03:41 AM
[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...
nmrlearner
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08-22-2010 03:33 AM
[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...
nmrlearner
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08-22-2010 03:33 AM
[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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08-22-2010 03:29 AM
[NMR paper] Structural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectros
Structural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectroscopy study.
Related Articles Structural 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...
Features of an NMR spectrum
Linear Mode
