The Hofmeister series categorizes ions based on their effects on protein stability, yet the microscopic mechanism remains a mystery. In this series, NaCl is neutral, Na(2)SO(4) and Na(2)HPO(4) are kosmotropic, while GdmCl and NaSCN are chaotropic. This study employs CD and NMR to investigate the effects of NaCl, Na(2)SO(4), and Na(2)HPO(4) on the conformation, stability, binding, and backbone dynamics (ps-ns and µs-ms time scales) of the WW4 domain with a high stability and accessible side...
Succinyl-DOTOPA: An effective triradical dopant for low-temperature dynamic nuclear polarization with high solubility in aqueous solvent mixtures at neutral pH
From The DNP-NMR Blog:
Succinyl-DOTOPA: An effective triradical dopant for low-temperature dynamic nuclear polarization with high solubility in aqueous solvent mixtures at neutral pH
Yau, Wai-Ming, Jaekyun Jeon, and Robert Tycko. “Succinyl-DOTOPA: An Effective Triradical Dopant for Low-Temperature Dynamic Nuclear Polarization with High Solubility in Aqueous Solvent Mixtures at Neutral PH.” Journal of Magnetic Resonance 311 (February 2020): 106672.
https://doi.org/10.1016/j.jmr.2019.106672.
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03-07-2020 06:20 PM
[NMR paper] NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration.
NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration.
Related Articles NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration.
Biochem Biophys Res Commun. 2016 Nov 14;:
Authors: Lee AR, Seo YJ, Choi SR, Ryu KS, Cheong HK, Lee SS, Park CJ, Lee JH
Abstract
A Z-DNA binding protein (ZBP)-containing protein kinase (PKZ) in fish species has an important role in the innate immune response. Previous structural studies of the Z? domain of the PKZ...
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11-20-2016 09:20 PM
NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration
NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration
Publication date: Available online 14 November 2016
Source:Biochemical and Biophysical Research Communications</br>
Author(s): Ae-Ree Lee, Yeo-Jin Seo, Seo-Ree Choi, Kyoung-Seok Ryu, Hae-Kap Cheong, Shim Sung Lee, Chin-Ju Park, Joon-Hwa Lee</br>
A Z-DNA binding protein (ZBP)-containing protein kinase (PKZ) in fish species has an important role in the innate immune response. Previous structural studies of the Z? domain of the PKZ from Carassius auratus...
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11-19-2016 08:35 PM
Nuclear Magnetic Resonance: A Dynamic View of Life - GotScience.org
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcTD3VjUnuZKDQD01jRAwdLJ50T9dMFEYJv7WHJkqS5ybdx2h3mQblEk7nz1kDuyZCR0D4cItvcx
GotScience.org
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Nuclear Magnetic Resonance: A Dynamic View of Life
GotScience.org
Florian Celli is a PhD student of biophysics in the Center for Atomic Energy (CEA of Saclay) and the Synchrotron SOLEIL in Paris. He uses nuclear magnetic resonance to study protein dynamics in order to understand their biological role. He co-writes 2 ...
Nuclear Magnetic Resonance: A Dynamic View of Life - GotScience.org
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05-11-2016 06:13 AM
[NMR paper] Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
J Biomol NMR. 2013 Sep 7;
Authors: Tumulka F, Roos C, Löhr F, Bock C, Bernhard F, Dötsch V, Abele R
Abstract
The ATP binding cassette transporter TAPL translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP. Functionally, this transporter can be...
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09-10-2013 08:44 PM
[NMR paper] A novel view of domain flexibility in E. coli adenylate kinase based on structural mo
A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
Related Articles A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
J Mol Biol. 2002 Jan 11;315(2):155-70
Authors: Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E
Adenylate kinase from Escherichia coli (AKeco), consisting of a single 23.6 kDa polypeptide chain folded into domains CORE, AMPbd and LID, catalyzes the reaction AMP+ATP-->2ADP. In the...
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11-24-2010 08:49 PM
[NMR paper] Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Related Articles Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion...