[NMR paper] Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Related Articles Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Biophys J. 2017 May 09;112(9):1820-1828
Authors: Kawamura T, Wakamoto T, Kitazawa S, Sakuraba S, Kameda T, Kitahara R
Abstract
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic...
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05-13-2017 02:08 PM
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Publication date: 9 May 2017
Source:Biophysical Journal, Volume 112, Issue 9</br>
Author(s): Takahiro Kawamura, Takuro Wakamoto, Soichiro Kitazawa, Shun Sakuraba, Tomoshi Kameda, Ryo Kitahara</br>
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic relaxation enhancements (PREs) on amide groups of proteins in solution. Outer...
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05-10-2017 06:52 AM
[NMR paper] Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
Escherichia coli topoisomerase IV E subunit and an inhibitor binding mode revealed by NMR spectroscopy.
J Biol Chem. 2016 Jun 30;
Authors: Li Y, Wong YL, Ng FM, Liu B, Wong YX, Poh ZY, Liu S, Then SW, Lee MY, Ng HQ, Huang Q, Hung AW, Cherian J, Hill J, Keller TH, Kang C
Abstract
Bacterial topoisomerases are attractive antibacterial drug targets due to their importance in bacterial growth and low homology with other human...
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07-02-2016 07:23 PM
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets
Wan-Na Chen, Christoph Nitsche, Kala Bharath Pilla, Bim Graham, Thomas Huber, Christian D. Klein and Gottfried Otting
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b00416/20160324/images/medium/ja-2016-004167_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b00416
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/yfHNdUxBP5M
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03-25-2016 04:12 PM
[NMR paper] Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets.
J Am Chem Soc. 2016 Mar 14;
Authors: Chen WN, Nitsche C, Pilla KB, Graham B, Huber T, Klein CD, Otting G
Abstract
Structure-guided drug design relies on detailed structural knowledge of protein-ligand complexes, but crystallization of co-complexes is not always possible. Here we present a sensitive nuclear...
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03-15-2016 11:57 AM
New analysis shows how proteins shift into working mode - Phys.Org
<img alt="" height="1" width="1" />
New analysis shows how proteins shift into working mode
Phys.Org
For more than 50 years, scientists around the world have combined experimental techniques such as X-ray crystallography and nuclear magnetic resonance imaging with computer algorithms to determine the three-dimensional structure of proteins.
New analysis shows how proteins shift into working mode - Phys.Org
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08-09-2013 08:00 PM
New analysis shows how proteins shift into working mode - R & D Magazine
New analysis shows how proteins shift into working mode - R & D Magazine
http://www.bionmr.com//t3.gstatic.com/images?q=tbn:ANd9GcRhYu4PjLfd1Y18f6IXT8akbhG3ayESvhDd3heK-FJhvszFTafquWUQ3gbKsRBulqrzKo8M2hAo
R & D Magazine
<img alt="" height="1" width="1" />
New analysis shows how proteins shift into working mode
R & D Magazine
One, cyclophilin A, can facilitate protein folding, while the other, dihydrofolate reductase (dhfr), helps regulate cell proliferation and cell growth. Their method, for the first time, provides an atomically detailed structural framework for the dhfr ...
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08-08-2013 03:46 PM
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
Abstract Zinc is the second most abundant metal ion incorporated in proteins, and is in many cases a crucial component of protein three-dimensional structures. Zinc ions are frequently coordinated by cysteine and histidine residues. Whereas cysteines bind to zinc via their unique Sγ atom, histidines can coordinate zinc with two different coordination modes, either Nδ1 or Nε2 is coordinating the zinc ion. The determination of this coordination mode is crucial for the accurate...