Related ArticlesProton NMR comparison of noncovalent and covalently cross-linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c.
Proton NMR spectroscopy at 500 and 361 MHz has been used to characterize the noncovalent or electrostatic complexes of yeast cytochrome c peroxidase (CcP) with horse, tuna, yeast isozyme-1, and yeast isozyme-2 ferricytochromes c and the covalently cross-linked complexes of cytochrome c peroxidase with horse and yeast isozyme-1 ferricytochromes c. Under the conditions employed in this work, the stoichiometry of the predominant complex formed in solution (which totaled greater than 90% of complex formed) was found to be 1:1 in all cases. These studies have elucidated significant differences in the proton NMR absorption spectra and the one-dimensional nuclear Overhauser effect difference spectra of the complexes, depending on the specific species of ferricytochrome c incorporated. In particular, the results indicate that the noncovalent complexes formed between CcP and physiological redox partners (yeast isozyme-1 or yeast isozyme-2 ferricytochromes c) are distinctly different from the noncovalent complexes formed between CcP and ferricytochromes c from horse and tuna. Parallel chemical cross-linking studies carried out using mixtures of cytochrome c peroxidase with horse ferricytochrome c, and cytochrome c peroxidase with yeast isozyme-1 ferricytochrome c further emphasize such cytochrome c-dependent differences, with only the covalently cross-linked complex of physiological redox partners (cytochrome c peroxidase/yeast isozyme-1) displaying NMR spectra characteristic of a heterogeneous mixture of different 1:1 complexes. Finally, one-dimensional nuclear Overhauser effect experiments have proven valuable in selectively and efficiently probing the protein-protein interface in these complexes, including the environment around the cytochrome c heme 3-methyl group and Phe-82.
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 2 July 2011</br>
Wenxing, Tang , Alexander A., Nevzorov</br>
Thermodynamic limit of magnetization corresponding to the intact proton bath often cannot be transferred in a single cross-polarization contact. This is mainly due to the finite ratio between the number densities of the high-...
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[NMR paper] Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HI
Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides.
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Biochemistry. 2003 Apr 1;42(12):3527-35
Authors: Yang R, Yang J, Weliky DP
In the HIV-1 gp41 and other viral fusion proteins, the minimal oligomerization state is believed to be trimeric with three N-terminal fusion peptides inserting into the membrane in close proximity. Previous studies have demonstrated that the...
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[NMR paper] Fabrication of homogeneously cross-linked, functional alginate microcapsules validate
Fabrication of homogeneously cross-linked, functional alginate microcapsules validated by NMR-, CLSM- and AFM-imaging.
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Biomaterials. 2003 May;24(12):2083-96
Authors: Zimmermann H, Hillgärtner M, Manz B, Feilen P, Brunnenmeier F, Leinfelder U, Weber M, Cramer H, Schneider S, Hendrich C, Volke F, Zimmermann U
Cross-linked alginate microcapsules of sufficient mechanical strength can immunoisolate cells for the...
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[NMR paper] A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY i
A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides.
Related Articles A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides.
J Biomol NMR. 2002 Jul;23(3):181-94
Authors: Feenstra KA, Peter C, Scheek RM, van Gunsteren WF, Mark AE
Three methods for calculating nuclear magnetic resonance cross-relaxation rates from molecular dynamics simulations of small flexible molecules have been compared in terms of their ability to...
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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...
[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...
Proton NMR comparison of noncovalent and covalently cross-linked complexes of cytochr
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