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...
[NMR paper] Application of Solution NMR to Structural Studies on ?-Helical Integral Membrane Proteins.
Application of Solution NMR to Structural Studies on ?-Helical Integral Membrane Proteins.
Related Articles Application of Solution NMR to Structural Studies on ?-Helical Integral Membrane Proteins.
Molecules. 2017 Aug 15;22(8):
Authors: Sim DW, Lu Z, Won HS, Lee SN, Seo MD, Lee BJ, Kim JH
Abstract
A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To...
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[NMR paper] Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
J Am Chem Soc. 2017 Jun 14;
Authors: Good D, Pham C, Jagas J, Lewandowski JR, Ladizhansky V
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude...
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[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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[NMR paper] Solution NMR Structure Determination of Polytopic ?-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.
Solution NMR Structure Determination of Polytopic ?-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR Structure Determination of Polytopic ?-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.
Methods Enzymol. 2015;557:329-348
Authors: Columbus L, Kroncke B
Abstract
Solution nuclear...
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[NMR paper] Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Biochim Biophys Acta. 2013 Jul 2;
Authors: Gautier A
Abstract
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical...
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Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Publication date: Available online 2 July 2013
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics</br>
Author(s): Antoine Gautier</br>
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical reactions and mediate protein–protein interactions. Indeed, the...
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Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR
October 2012
Publication year: 2012
Source:Current Opinion in Structural Biology, Volume 22, Issue 5</br>
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Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation...
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02-03-2013 10:13 AM
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Curr Opin Struct Biol. 2011 Jul 18;
Authors: Nietlispach D, Gautier A
NMR spectroscopy has established itself as one of the main techniques for the structural study of integral membrane proteins. Remarkably, over the last few years, substantial progress has been achieved in the structure determination of increasingly complex polytopical ?-helical membrane proteins, with their size approaching ~100kDa. Such advances are the...
Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
Linear Mode
