[ASAP] A Nuclear Resonance Vibrational Spectroscopic Study of Oxy Myoglobins Reconstituted with Chemically Modified Heme Cofactors: Insights into the Fe–O2 Bonding and Internal Dynamics of the Protein
[ASAP] A Nuclear Resonance Vibrational Spectroscopic Study of Oxy Myoglobins Reconstituted with Chemically Modified Heme Cofactors: Insights into the Fe–O2 Bonding and Internal Dynamics of the Protein
[ASAP] Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor ?B RelA Subunit
Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor ?B RelA Subunit
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00158/20180510/images/medium/bi-2018-00158n_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00158
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05-11-2018 01:53 AM
[ASAP] Improved Method for the Incorporation of Heme Cofactors into Recombinant Proteins Using Escherichia coli Nissle 1917
Improved Method for the Incorporation of Heme Cofactors into Recombinant Proteins Using Escherichia coli Nissle 1917
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00242/20180425/images/medium/bi-2018-00242b_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00242
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04-26-2018 02:15 AM
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
From The DNP-NMR Blog:
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
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Oganesyan, V.S., et al., A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics. J. Magn. Reson., 2017. 274: p. 24-35.
www.sciencedirect.com/science/article/pii/S1090780716302270
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[NMR paper] A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
Publication date: January 2017
Source:Journal of Magnetic Resonance, Volume 274</br>
Author(s): Vasily S. Oganesyan, Fatima Chami, Gaye F. White, Andrew J. Thomson</br>
EPR studies combined with fully atomistic Molecular Dynamics (MD) simulations and an MD-EPR simulation method provide evidence for intrinsic low rotameric mobility of a nitroxyl spin label, Rn, compared to the more widely employed label MTSL (R1). Both experimental...
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11-19-2016 08:35 PM
[NMR paper] pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
J Phys Chem B. 2013 Apr 11;117(14):3689-706
Authors: Toal S, Meral D, Verbaro D, Urbanc B, Schweitzer-Stenner R
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09-24-2013 10:18 AM
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Biochim Biophys Acta. 2011 May 6;
Authors: Juillard S, Chevance S, Bondon A, Simonneaux G
The asymmetric 3-ethyl-2-methylporphyrin iron complex was synthetized and inserted into apomyoglobin. UV-visible spectroscopic studies demonstrated the capacity of iron to coordinate different exogenous axial ligands in ferrous and...
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05-24-2011 12:00 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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[NMR paper] Orientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE a
Orientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE and MATDUHM NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Orientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE and MATDUHM NMR.
Biochim Biophys Acta. 1992 Apr 8;1120(2):173-82
Authors: Yamamoto Y, Iwafune K, Nanai N, Chûjô R, Inoue Y, Suzuki T
The heme vinyl substituents in a shark (Galeorhinus japonicus) myoglobin in its met-cyano form (MbCN)...