The present and future of solution NMR in investigating the structure and dynamics of channels and transporters.
Curr Opin Struct Biol. 2013 Apr 26;
Authors: Oxenoid K, Chou JJ
Abstract
Membrane channels, transporters and receptors constitute essential means for cells to maintain homeostasis and communicate with the surroundings. Investigation of their molecular architecture and the dynamic process of transporting substrate or transmitting signals across the membrane barrier has been one of the frontiers in biomedical research. The past decade has seen numerous successes in the use of X-ray or electron crystallography in determining atomic-resolution structures of membrane proteins, and in some cases, even snapshots of different physiological states of the same protein have been obtained. But there are also many cases in which long-standing efforts to crystallize proteins have yet to succeed. Therefore we have practical needs for developing complementary biophysical tools such as NMR spectroscopy and electron microscopy for tackling these systems. This paper provides a number of key examples where the utility of solution NMR was pivotal in providing structural and functional information on ion channels and transporters.
PMID: 23628285 [PubMed - as supplied by publisher]
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Abstract CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability...
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05-01-2011 04:48 AM
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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02-08-2011 06:28 PM
[NMR paper] NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migrat
NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III.
Related Articles NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III.
J Biol Chem. 2003 Jun 6;278(23):21212-20
Authors: Fan D, Zheng Y, Yang D, Wang J
We report here the NMR structure and backbone dynamics of an exchangeable apolipoprotein, apoLp-III, from the insect Locusta migratoria. The NMR structure adopts an up-and-down elongated five-helix bundle, which is similar to the...
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11-24-2010 09:01 PM
[NMR paper] Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alp
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
Related Articles Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J Mol Biol. 2001 Sep 28;312(4):833-47
Authors: Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE
Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and...
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11-19-2010 08:44 PM
[NMR paper] Investigating the structure and properties of hydrated hydroxypropyl methylcellulose
Investigating the structure and properties of hydrated hydroxypropyl methylcellulose and egg albumin matrices containing carbamazepine: EPR and NMR study.
Related Articles Investigating the structure and properties of hydrated hydroxypropyl methylcellulose and egg albumin matrices containing carbamazepine: EPR and NMR study.
Pharm Res. 2000 Oct;17(10):1299-308
Authors: Katzhendler I, Mäder K, Azoury R, Friedman M
PURPOSE: The present study was conducted in order to investigate the correlation between the hydration properties of HPMC and EA...
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11-19-2010 08:29 PM
[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
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08-22-2010 03:33 AM
[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
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08-22-2010 03:33 AM
[Ryan's blog] From FID to Structure in 30 Minutes? Investigating the CASE Limiting Step
Source: Ryan's blog
From FID to Structure in 30 Minutes? Investigating the CASE Limiting Step
In yesterday's post I pointed you to an article that has become the most accessed article of all time in the Journal of Cheminformatics, co-authored by representatives of ACD/Labs. This article is a very comprehensive outline of the different approaches,...
The present and future of solution NMR in investigating the structure and dynamics of channels and transporters.
Linear Mode
