[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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http://feeds.feedburner.com/~r/acs/bichaw/~4/xEMFb1XNf30
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04-26-2018 02:15 AM
[ASAP] Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00019/20180410/images/medium/bi-2018-00019w_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00019
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http://feeds.feedburner.com/~r/acs/bichaw/~4/kty9sAc251I
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04-12-2018 01:01 AM
[ASAP] Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00072/20180409/images/medium/bi-2017-00072x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00072
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http://feeds.feedburner.com/~r/acs/bichaw/~4/4KHGVmMLJ6o
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04-10-2018 12:35 AM
[ASAP] Quantitative Characterization of Bivalent Probes for a Dual Bromodomain Protein, Transcription Initiation Factor TFIID Subunit 1
Quantitative Characterization of Bivalent Probes for a Dual Bromodomain Protein, Transcription Initiation Factor TFIID Subunit 1
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00150/20180328/images/medium/bi-2018-00150k_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00150
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http://feeds.feedburner.com/~r/acs/bichaw/~4/wc2_SENodAA
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03-29-2018 05:39 AM
T1 - Dynamic Nuclear Polarization Signal Enhancement with High-Affinity Biradical Tags #DNPNMR
From The DNP-NMR Blog:
T1 - Dynamic Nuclear Polarization Signal Enhancement with High-Affinity Biradical Tags #DNPNMR
Rivkah Rogawski, Ivan V. Sergeyev, Yongjun Li, M. Francesca Ottaviani, Virginia Cornish, and Ann E. McDermott The Journal of Physical Chemistry B 2017 121 (6), 1169-1175
http://dx.doi.org/10.1021/acs.jpcb.6b09021
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05-19-2017 04:40 PM
[NMR paper] Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel ?4 subunit: A low affinity interaction is required for inhibition of Cav2.1 Ca2+ currents.
FASEB J. 2015 Jan 6;
Authors: Xu X, Zhang F, Zamponi GW, Horne WA
Abstract
Rem, Rad, Kir/Gem (RGK) proteins, including Rem2, mediate profound inhibition of high-voltage activated Ca(2+) channels...
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01-08-2015 01:29 PM
[NMR paper] Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR rela
Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information.
Related Articles Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information.
J Biomol NMR. 2004 Jun;29(2):175-85
Authors: Jensen MR, Lauritzen C, Dahl SW, Pedersen J, Led JJ
The binding ability of a protein with a metal binding tag towards Ni(2+) was investigated by longitudinal paramagnetic NMR...
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11-24-2010 09:51 PM
[NMR paper] Conformational characteristics of high affinity Sp1 binding enhancer elements of HIV-
Conformational characteristics of high affinity Sp1 binding enhancer elements of HIV-LTR by high resolution 2D-NMR.
Related Articles Conformational characteristics of high affinity Sp1 binding enhancer elements of HIV-LTR by high resolution 2D-NMR.
J Biomol Struct Dyn. 1995 Dec;13(3):553-64
Authors: Singh MP, Pon RT, Lown JW
The understanding of early events in the expression of genes has vastly improved in recent years with the identification of a variety of gene- and sequence-specific DNA binding transcription factors. One such protein, Sp1,...
![[ASAP] Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor ?B RelA Subunit](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-protein-cofactors-essential-high-affinity-dna-binding-nuclear-factor-b-rela-subunit_ltr.gif)
[ASAP] Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor ?B RelA Subunit
Linear Mode
