[ASAP] Binding Affinity and Function of the Extremely Disordered Protein Complex Containing Human Linker Histone H1.0 and Its Chaperone ProTa
Binding Affinity and Function of the Extremely Disordered Protein Complex Containing Human Linker Histone H1.0 and Its Chaperone ProTa
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b01075/20181119/images/medium/bi-2018-01075n_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b01075
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http://feeds.feedburner.com/~r/acs/bichaw/~4/uyaYq1aE9Ks
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nmrlearner
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11-25-2018 06:02 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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nmrlearner
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04-10-2018 12:35 AM
[NMR paper] Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group
Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group
Iron(III)-5,15-diphenylporphyrin (1) and its derivatives (2-7) were accommodated by the heme acquisition protein HasA secreted by Pseudomonas aeruginosa, despite possessing bulky substituents at the meso-position of the porphyrin. Crystal structure analysis revealed that the two phenyl groups at the meso-positions of porphyrin extend outside HasA. It was shown that growth of P. aeruginosa was inhibited in the...
nmrlearner
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09-16-2017 09:58 PM
[NMR paper] NMR-based metabolomics reveals the metabolite profiles of Vibrio parahaemolyticus under ferric iron stimulation.
NMR-based metabolomics reveals the metabolite profiles of Vibrio parahaemolyticus under ferric iron stimulation.
Related Articles NMR-based metabolomics reveals the metabolite profiles of Vibrio parahaemolyticus under ferric iron stimulation.
J Microbiol. 2017 Aug;55(8):628-634
Authors: Zhou J, Lu C, Zhang D, Ma C, Su X
Abstract
Vibrio parahaemolyticus is a halophilic bacterium endemic to coastal areas, and its pathogenicity has caused widespread seafood poisoning. In our previous research, the protein expression of V....
nmrlearner
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07-29-2017 10:35 AM
[NMR paper] (1)H, (13)C and (15)N NMR assignments of an unusual Ca(2+)-binding protein from Entamoeba histolytica in its apo form.
(1)H, (13)C and (15)N NMR assignments of an unusual Ca(2+)-binding protein from Entamoeba histolytica in its apo form.
Related Articles (1)H, (13)C and (15)N NMR assignments of an unusual Ca(2+)-binding protein from Entamoeba histolytica in its apo form.
Biomol NMR Assign. 2016 Dec 19;
Authors: Verma D, Sakuntala M, Murmu A, Bhattacharya A, Chary KV
Abstract
We report almost complete sequence specific (1)H, (13)C and (15)N NMR assignments of an unusual Ca(2+)-binding protein from Entamoeba histolytica (EhCaBP6) in its apo form as...
nmrlearner
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12-19-2016 07:58 PM
[NMR paper] 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of he
13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
Related Articles 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
J Am Chem Soc. 2002 May 29;124(21):5936-7
Authors: Fujii H
13CN ion appears to have the greatest potential to probe the heme environment of the ferric heme proteins; however, a resonance of the iron-bound (13)CN ion in ferric heme proteins has not yet been located. We show here the first detection of (13)C NMR signals of the...
nmrlearner
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11-24-2010 08:49 PM
[NMR paper] NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro
NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
Related Articles NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
J Mol Biol. 2000 Jan 28;295(4):729-36
Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E
The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR....
nmrlearner
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11-18-2010 09:15 PM
[NMR paper] Three-dimensional structure of bovine heart fatty-acid-binding protein with bound pal
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
Eur J Biochem. 1995 May 15;230(1):266-80
Authors: Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM,...
![[ASAP] Crystal Structure of the Siderophore Binding Protein BauB Bound to an Unusual 2:1 Complex Between Acinetobactin and Ferric Iron](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-crystal-structure-siderophore-binding-protein-baub-bound-unusual-2-1-complex-between-acinetobactin-ferric-iron_ltr.gif)
[ASAP] Crystal Structure of the Siderophore Binding Protein BauB Bound to an Unusual 2:1 Complex Between Acinetobactin and Ferric Iron
Linear Mode
