Related Articles13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
Eur J Biochem. 1992 Jun 15;206(3):721-8
Authors: Santos H, Turner DL
The CHn groups in the aliphatic side chains of horse cytochrome c have been characterized according to the chemical shifts of both 13C-NMR and 1H-NMR signals, their temperature dependence and the number of attached protons, n. The primary assignments of resonances from the 55 side-chain methyl and the 27 methine groups were obtained directly for the oxidised and the reduced forms. Specific assignments of the 13C resonances were obtained through shift-correlation experiments and comparison with earlier 1H-NMR studies, by further measurements of proton-proton interactions, or by elimination. Comparison of the paramagnetic shifts of carbon and protons indicates a small redox-related change of conformation in the vicinity of Trp59 and a significant expansion of the protein over 30-50 degrees C.
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Abstract Methyl-transverse relaxation optimized spectroscopy is rapidly becoming the preferred NMR technique for probing structure and dynamics of very large proteins up to ~1 MDa in molecular size. Data interpretation, however, necessitates assignment of methyl groups which still presents a very challenging and time-consuming process. Here we demonstrate that, in combination with a known 3D structure, paramagnetic...
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09-26-2011 06:42 AM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies
Abstract Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance assignment of methyl probes in high molecular weight protein assemblies can be efficiently achieved by combining fast NMR experiments, residue-type-specific isotope-labeling and automated site-directed mutagenesis. The utility of this general and straightforward strategy is demonstrated through...
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06-06-2011 12:53 AM
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR. 2011 May 29;
Authors: Amero C, Asunción Durá M, Noirclerc-Savoye M, Perollier A, Gallet B, Plevin MJ, Vernet T, Franzetti B, Boisbouvier J
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance...
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06-01-2011 02:30 PM
[NMR paper] Proton NMR study of chemically modified horse heart ferricytochrome c confirms the pr
Proton NMR study of chemically modified horse heart ferricytochrome c confirms the presence of histidine and lysine-ligated conformers in 30% acetonitrile solution.
Related Articles Proton NMR study of chemically modified horse heart ferricytochrome c confirms the presence of histidine and lysine-ligated conformers in 30% acetonitrile solution.
J Inorg Biochem. 2003 Apr 1;94(4):381-5
Authors: Sivakolundu SG, Mabrouk PA
Comparison of the 1H NMR spectra for guanidinated ferricyt c and chloro(terpyridine)platinum(II)-modified ferricyt c in 30%...
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11-24-2010 09:01 PM
[NMR paper] Protein hydration and location of water molecules in oxidized horse heart cytochrome
Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
Related Articles Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
J Magn Reson. 2000 Nov;147(1):1-8
Authors: Bertini I, Huber JG, Luchinat C, Piccioli M
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by (1)H NMR spectroscopy. Two-dimensional, homonuclear ePHOGSY-NOESY experiments are used to map water-protein interactions. The detected NOEs reveal...
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11-19-2010 08:29 PM
[NMR paper] A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas ace
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.
Related Articles A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.
Eur J Biochem. 1999 Dec;266(2):634-43
Authors: Assfalg M, Banci L, Bertini I, Bruschi M, Giudici-Orticoni MT, Turano P
The solution structure via 1H NMR of the fully reduced form of cytochrome c7 has been obtained. The protein...
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11-18-2010 08:31 PM
[NMR paper] Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c
Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
Related Articles Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
Proteins. 1998 Aug 1;32(2):241-7
Authors: Bhuyan AK, Udgaonkar JB
A procedure to measure exchange rates of fast exchanging protein amide hydrogens by time-resolved NMR spectroscopy following in situ initiation of the reaction by diluting a native protein solution into an...
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11-17-2010 11:15 PM
KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
Naohiro Kobayashi, Junji Iwahara, Seizo Koshiba, Tadashi Tomizawa, Naoya Tochio, Peter Güntert, Takanori Kigawa and Shigeyuki Yokoyama
Journal of Biomolecular NMR; 2007; 39(1) pp 31 - 52
Abstract:
The recent expansion of structural genomics has increased the demands for quick and accurate protein structure determination by NMR spectroscopy. The conventional strategy without an automated protocol can no longer satisfy the needs of high-throughput...
13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and
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