Morphology and magnetic structure of the ferritin core during iron loading and releasing by magnetooptical and NMR methods.
ACS Appl Mater Interfaces. 2018 Feb 08;:
Authors: Koralewski M, Balej?íková L, Mitroova Z, Pochylski M, Baranowski M, Kopcansky P
Abstract
The ferritin is a protein, which serves as a storage and transportation capsule for iron inside living organisms. Continuous charging protein with iron and releasing it from the ferritin is necessary to assure proper management of this important ions within organism. From other side synthetic ferritin have great potential for biomedical and technological applications. In this work the behavior of ferritin during the processes of iron loading and releasing was examined using multiplicity of experimental technique. The quality of protein's shell was monitored using circular dichroism, whereas the average size and its distribution was estimated from dynamic light scattering and TEM images, respectively. Because of the magnetic behavior of the iron mineral, number of magnetooptical methods were used to gain information on the iron core of the ferritin. Faraday rotation and magnetic linear birefringence studies provides evidence that the iron loading and the iron release processes are not symmetrical. The spatial organization of the mineral within the protein's core changes depending on whether the iron was incorporated to, or removed from the ferritins shell. Magnetic optical rotatory dispersion spectra exclude contribution of Fe(II)-composed mineral, whereas joined magnetooptical and NMR results indicate that no mineral with high magnetization appear at any stage of the loading/release process. These findings suggest that the iron core of loaded/released ferritin consists of single-phase i.e. ferrihydrite. Presented results demonstrate usefulness of emerging magnetooptical methods in biomedical research and applications.
PMID: 29417811 [PubMed - as supplied by publisher]
The Crystal Structure of a Maxi/Mini-Ferritin ChimeraReveals Guiding Principles for the Assembly of Protein Cages
The Crystal Structure of a Maxi/Mini-Ferritin ChimeraReveals Guiding Principles for the Assembly of Protein Cages
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00312/20170721/images/medium/bi-2017-00312m_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00312
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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nmrlearner
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07-22-2017 05:57 AM
Correlating Synthetic Methods, Morphology, Atomic-Level Structure, and Catalytic Activity of Sn-? Catalysts
From The DNP-NMR Blog:
Correlating Synthetic Methods, Morphology, Atomic-Level Structure, and Catalytic Activity of Sn-? Catalysts
Wolf, P., et al., Correlating Synthetic Methods, Morphology, Atomic-Level Structure, and Catalytic Activity of Sn-? Catalysts. ACS Catalysis, 2016. 6(7): p. 4047-4063.
http://dx.doi.org/10.1021/acscatal.6b00114
[NMR paper] Solution and Solid State NMR Approaches To Draw Iron Pathways in the Ferritin Nanocage.
Solution and Solid State NMR Approaches To Draw Iron Pathways in the Ferritin Nanocage.
Solution and Solid State NMR Approaches To Draw Iron Pathways in the Ferritin Nanocage.
Acc Chem Res. 2013 Sep 3;
Authors: Lalli D, Turano P
Abstract
Ferritins are intracellular proteins that can store thousands of iron(III) ions as a solid mineral. These structures autoassemble from four-helix bundle subunits to form a hollow sphere and are a prototypical example of protein nanocages. The protein acts as a reservoir, encapsulating iron as ferric oxide...
nmrlearner
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09-05-2013 01:07 PM
[NMR paper] Solution NMR structure investigation for releasing mechanism of neocarzinostatin chro
Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein.
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J Biol Chem. 2005 Mar 25;280(12):11340-6
Authors: Takashima H, Yoshida T, Ishino T, Hasuda K, Ohkubo T, Kobayashi Y
Holo-neocarzinostatin (holo-NCS) is a complex protein carrying the anti-tumor active enediyne ring chromophore by a scaffold consisting of an immunoglobulin-like seven-stranded...
nmrlearner
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11-24-2010 11:14 PM
[NMR paper] Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
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J Inorg Biochem. 1998 Sep;71(3-4):153-7
Authors: Vymazal J, Brooks RA, Bulte JW, Gordon D, Aisen P
Twenty ferritin samples were prepared at pH 6.5 with average loadings of 0-89 Fe atoms per molecule. Nuclear magnetic relaxation times T1 and T2 were measured at 3 degrees C, 23 degrees C, and at 37 degrees C and at field strength from 0.025 to 1.5 T. The field dependence, temperature dependence,...
nmrlearner
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11-17-2010 11:15 PM
NMR structure of the first extracellular domain of corticotropin releasing factor rec
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J Biol Chem. 2010 Sep 15;
Authors: Grace CR, Perrin MH, Gulyas J, Rivier JE, Vale WW, Riek R
The corticotropin releasing factor (CRF) peptide hormone family members coordinate endocrine, behavioral, autonomic and metabolic responses to...
nmrlearner
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09-17-2010 04:14 PM
Installation of GROMACS 3.3.1 on Dell Inspiron 6400 with Fedora Core 6, Test 3, Dual Core processor
This is not really a "hard-core NMR topic" but it could be useful for people who try to complement dynamics data from NMR relaxation experiments with MD simulations.
I had really hard time trying to install the newer versions of Gromacs 3.3 and 3.3.1 on my laptop (Dell Inspiron 6400 Dual Core processor) . The laptop used to run Suse 10.1 that was recently replaced with Fedora Core 6 Test 3 (that finally supports Intel integrated mobile 945 video cards). With both OS, Gromacs 3.3.x could be installed, however, its sub-program "genion" failed (the program never ends while consuming 100%...