[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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nmrlearner
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05-11-2018 01:53 AM
[ASAP] Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems
Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01275/20180404/images/medium/bi-2017-012754_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01275
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nmrlearner
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04-06-2018 01:51 AM
Manipulating Protein–Protein Interactions inNonribosomal Peptide Synthetase Type II Peptidyl Carrier Proteins
Manipulating Protein–Protein Interactions inNonribosomal Peptide Synthetase Type II Peptidyl Carrier Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00884/20171002/images/medium/bi-2017-00884r_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00884
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nmrlearner
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10-03-2017 03:24 AM
[NMR paper] Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Related Articles Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.
Nucleic Acids Res. 2015 Jan 13;
Authors: Collins KM, Oregioni A, Robertson LE, Kelly G, Ramos A
Abstract
Defining the RNA target selectivity of the proteins regulating mRNA metabolism is a key issue in RNA biology. Here we present a novel use of principal component analysis (PCA) to extract the RNA sequence preference of RNA binding...
nmrlearner
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01-15-2015 06:10 PM
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
J Mol Biol. 2011 Apr 12;
Authors: Mizuno S, Amida H, Kobayashi N, Aizawa SI, Tate SI
The flagellar cytoplasmic protein FliK controls hook elongation by two successive events: by determining hook length and by stopping the supply of hook protein. These two distinct roles are assigned to different...
nmrlearner
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04-25-2011 11:53 AM
[NMR paper] High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli d
High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Related Articles High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Biochemistry. 2000 Oct 24;39(42):12789-95
Authors: Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K
A high-pressure (15)N/(1)H two-dimensional NMR study has been carried out on folate-bound dihydrofolate reductase (DHFR) from Escherichia coli in the pressure range between 30 and 2000 bar. Several...
nmrlearner
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11-19-2010 08:29 PM
[NMR paper] Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of
Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Related Articles Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Biochem Biophys Res Commun. 2000 Mar 16;269(2):387-92
Authors: Panchal SC, Hosur RV
HIV I protease has been the target of extensive and variety of investigations in recent years because of its importance in the AIDS viral life cycle. We...
nmrlearner
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11-18-2010 09:15 PM
[NMR paper] Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical a
Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Related Articles Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Biochemistry. 1993 Jan 12;32(1):282-9
Authors: Adler M, Carter P, Lazarus RA, Wagner G
The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet...
![[ASAP] Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-hinge-type-dimerization-proteins-tetracysteine-peptide-high-pairing-specificity_ltr.gif)
[ASAP] Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity
Linear Mode
