[NMR paper] Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution......
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[NMR paper] 19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
Related Articles 19F NMR as a versatile tool to study (membrane) protein structure and dynamics.
Biol Chem. 2018 Dec 01;:
Authors: Rose-Sperling D, Tran MA, Lauth LM, Goretzki B, Hellmich UA
Abstract
To elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as...
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04-21-2019 08:38 PM
Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles #DNPNMR
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Masion, A., et al., Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles. Sci Rep, 2017. 7(1): p. 3430.
https://www.ncbi.nlm.nih.gov/pubmed/28611402
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08-07-2017 07:31 PM
Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles #DNPNMR
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Masion, A., et al., Dynamic Nuclear Polarization NMR as a new tool to investigate the nature of organic compounds occluded in plant silica particles. Sci Rep, 2017. 7(1): p. 3430.
https://www.ncbi.nlm.nih.gov/pubmed/28611402
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07-10-2017 02:13 PM
[NMR paper] NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
NMR as a tool to investigate the structure, dynamics and function of membrane proteins.
Nat Struct Mol Biol. 2016 Jun 7;23(6):468-474
Authors: Liang B, Tamm LK
Abstract
Membrane-protein NMR occupies a unique niche for determining structures, assessing dynamics, examining folding, and studying the binding of lipids, ligands and drugs to membrane proteins. However, NMR analyses of membrane proteins also face special challenges that are not...
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06-09-2016 07:44 PM
[NMR paper] Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin.
Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin.
PLoS One. 2015;10(3):e0122444
Authors: ...
[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
NMR as a tool to investigate the structure, dynamics and function of membrane proteins - Nature.com
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