Related ArticlesNMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins.
FEBS Lett. 2002 Jul 31;524(1-3):177-82
Authors: Shekhtman A, Ghose R, Goger M, Cowburn D
We present here a stable isotope labeling technique for proteins, which seeks the appropriate compromise between the advantages of (a) random isotope labeling, with its large number of protons available for structure determination, and (b) selective labeling to generate isolated proton spins decreasing spectral complexity and improving relaxation properties of NMR experiments. The described reduced proton (REDPRO) procedure results in side-chain specific protonation of overexpressed proteins, which is highly selective. The REDPRO labeling scheme provides a sufficient number of NOE constraints for structure calculation. Dramatically improved relaxation properties of the heteronuclear magnetization transfer coupled with TROSY advantages make the proposed labeling scheme an attractive approach for study of high molecular weight protein targets, their ligand sites, and interdomain interactions.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
Chemphyschem. 2011 Apr 4;12(5):915-8
Authors: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH
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[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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[NMR paper] Proton NMR investigation of the heme active site structure of an engineered cytochrom
Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Related Articles Proton NMR investigation of the heme active site structure of an engineered cytochrome c peroxidase that mimics manganese peroxidase.
Biochemistry. 1999 Jul 13;38(28):9146-57
Authors: Wang X, Lu Y
The heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese peroxidase (MnP) has been characterized by both one- and two-dimensional NMR spectroscopy. All...
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[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Biochemistry. 1995 Dec 5;34(48):15646-53
Authors: Lanzilotta WN, Holz RC, Seefeldt LC
This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
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[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
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[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
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[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from
1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
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 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
Eur J Biochem. 1993 Feb 15;212(1):69-78
Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M
1H one-dimensional and two-dimensional NMR spectra have been...
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[NMR paper] Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cy
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
Related Articles Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
J Biomol NMR. 1991 Jul;1(2):145-54
Authors: Gooley PR, Zhao D, MacKenzie NE
The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were...