[NMR paper] Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Related Articles Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
J Mol Biol. 2017 May 20;:
Authors: Mandala VS, Liao SY, Kwon B, Hong M
Abstract
The influenza M2 protein forms an acid-activated proton channel that is essential for virus replication. The transmembrane H37 selects for protons under low external pH (pHout) while W41...
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05-26-2017 08:36 PM
[NMR paper] Beyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.
Beyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.
Related Articles Beyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.
J Phys Chem B. 2017 Apr 20;:
Authors: Qin H, Miao Y, Cross TA, Fu R
Abstract
In terms of structural biology, solid-state NMR experiments and strategies have been well established for resonance assignments leading to the...
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04-21-2017 03:35 PM
[NMR paper] Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-molecule force spectroscopy (SMFS) has become a powerful tool in investigating the mechanical unfolding/folding of proteins at the single-molecule level. Polyproteins made of tandem identical repeats have been widely used in atomic force microscopy (AFM)-based SMFS studies, where polyproteins not only serve as fingerprints to identify single-molecule stretching events, but may also improve statistics of data...
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12-27-2016 11:04 PM
Ion Channel Formation by Tau Protein: Implicationsfor Alzheimer’s Disease and Tauopathies
Ion Channel Formation by Tau Protein: Implicationsfor Alzheimer’s Disease and Tauopathies
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00988/20151201/images/medium/bi-2015-009883_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00988
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/KDZc9KwazBE
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12-07-2015 06:38 PM
[NMR paper] Dehydration of Ions in Voltage-Gated Carbon Nanopores Observed by in situ NMR.
Dehydration of Ions in Voltage-Gated Carbon Nanopores Observed by in situ NMR.
Related Articles Dehydration of Ions in Voltage-Gated Carbon Nanopores Observed by in situ NMR.
J Phys Chem Lett. 2015 Dec 2;
Authors: Luo ZX, Xing YZ, Liu S, Ling YC, Kleinhammes A, Wu Y
Abstract
Ion transport through nanochannels is of fundamental importance in voltage-gated protein ion channels and energy storage devices. Direct microscopic observations are critical for understanding the intricacy of ionic processes in nanoconfinement. Here we...
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12-03-2015 07:37 PM
Single-Cell NMR? How About Single-Protein NMR? - Corante
Single-Cell NMR? How About Single-Protein NMR? - Corante
<img alt="" height="1" width="1" />
Single-Cell NMR? How About Single-Protein NMR?
Corante
Two different research teams have reported a completely different way to run NMR experiments, one that looks like it could take the resolution down to cellular (or even large protein) levels. These two papers in Science have the details (and there's an ...
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02-04-2013 08:00 PM
[NMR paper] Large structure rearrangement of colicin ia channel domain after membrane binding fro
Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR.
Related Articles Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR.
J Am Chem Soc. 2005 May 4;127(17):6402-8
Authors: Luo W, Yao X, Hong M
One of the main mechanisms of membrane protein folding is by spontaneous insertion into the lipid bilayer from the aqueous environment. The bacterial toxin, colicin Ia, is one such protein. To shed light on the conformational changes...
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11-25-2010 08:21 PM
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
Related Articles NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
J Biol Chem. 2010 Jul 28;
Authors: Montserret R, Saint N, Vanbelle C, Salvay AG, Simorre JP, Ebel C, Sapay N, Renisio JG, Bockmann A, Steinmann E, Pietschmann T, Dubuisson J, Chipot C, Penin F
The small membrane protein p7 of hepatitis C virus forms oligomers and exhibits ion channel activity essential for virus infectivity. These viroporin features render p7 an...
Aberrantly Large Single-Channel Conductance of PolyhistidineArm-Containing Protein Nanopores
Hybrid Mode
