Compared to soluble protein counterparts, the understanding of membrane protein stability, solvent interactions, and function are not as well understood. Recent advancements in labeling, expression, and stabilization of membrane proteins have enabled solution nuclear magnetic resonance spectroscopy to investigate membrane protein conformational states, ligand binding, lipid interactions, stability, and folding. This review highlights these advancements and new understandings and provides...
[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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08-17-2017 01:01 PM
[NMR paper] Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from E. coli.
J Biol Chem. 2014 Jun 23;
Authors: Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, Riek R
Abstract
The solution NMR structure of the ?-helical integral membrane protein YgaP from Escherichia coli in mixed DHPC-7/LMPG micelles is presented. In these micelles, YgaP forms a homo-dimer with the two transmembrane helices...
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06-25-2014 08:06 PM
[NMR paper] Advances in NMR structures of integral membrane proteins.
Advances in NMR structures of integral membrane proteins.
Advances in NMR structures of integral membrane proteins.
Curr Opin Struct Biol. 2013 May 27;
Authors: Maslennikov I, Choe S
Abstract
Integral membrane proteins (IMPs) play a central role in cell communication with the environment. Their structures are essential for our understanding of the molecular mechanisms of signaling and for drug design, yet they remain badly underrepresented in the protein structure databank. Solution NMR is, aside from X-ray crystallography, the major tool...
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Advances in NMR structures of integral membrane proteins
Advances in NMR structures of integral membrane proteins
Publication date: Available online 27 May 2013
Source:Current Opinion in Structural Biology</br>
Author(s): Innokentiy Maslennikov , Senyon Choe</br>
Integral membrane proteins (IMPs) play a central role in cell communication with the environment. Their structures are essential for our understanding of the molecular mechanisms of signaling and for drug design, yet they remain badly underrepresented in the protein structure databank. Solution NMR is, aside from X-ray crystallography, the major tool in...
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05-28-2013 06:24 AM
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Curr Opin Chem Biol. 2011 Jun 18;
Authors: Kang C, Li Q
Signals between a cell and its environment are often transmitted through membrane proteins; therefore, many membrane proteins, including G protein-coupled receptors (GPCRs) and ion channels, are important drug targets. Structural information about membrane proteins remains limited owing to challenges in protein expression, purification and the selection of membrane-mimicking systems that will...
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06-21-2011 01:50 PM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
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12-01-2010 06:56 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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11-24-2010 11:14 PM
[NMR paper] Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia
Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.
Related Articles Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.
FEBS Lett. 2001 Aug 31;504(3):173-8
Authors: Fernández C, Hilty C, Bonjour S, Adeishvili K, Pervushin K, Wüthrich K
Membrane proteins are usually solubilized in polar solvents by incorporation into micelles. Even for small membrane proteins these mixed micelles have rather large molecular masses, typically beyond 50000 Da. The NMR technique TROSY...
Solution NMR investigations of integral membrane proteins: Challenges and innovations
Linear Mode
