Related ArticlesNanodiscs and Solution NMR: preparation, application and challenges.
Nanotechnol Rev. 2017 Feb;6(1):111-126
Authors: Puthenveetil R, Nguyen K, Vinogradova O
Abstract
Nanodiscs provide an excellent system for the structure-function investigation of membrane proteins. Its direct advantage lies in presenting a water soluble form of an otherwise hydrophobic molecule, making it amenable to a plethora of solution techniques. Nuclear Magnetic Resonance is one such high resolution approach that looks at the structure and dynamics of a protein with atomic level precision. Recently, there has been a breakthrough in making nanodiscs more susceptible for structure determination by solution NMR, yet it still remains to become the preferred choice for a membrane mimetic. In this practical review, we provide a general discourse on nanodisc and its application to solution NMR. We also offer potential solutions to remediate the technical challenges associated with nanodisc preparation and the choice of proper experimental set-ups. Along with discussing several structural applications, we demonstrate an alternative use of nanodiscs for functional studies, where we investigated the phosphorylation of a cell surface receptor, Integrin. This is the first successful manifestation of observing activated receptor phosphorylation in nanodiscs through NMR. We additionally present an on-column method for nanodisc preparation with multiple strategies and discuss the potential use of alternative nanoscale phospholipid bilayer systems like SMA lipid discs and Saposin-A lipoprotein discs.
[NMR paper] Smaller*Nanodiscs are Suitable for Studying Protein Lipid Interactions by Solution NMR.
Smaller*Nanodiscs are Suitable for Studying Protein Lipid Interactions by Solution NMR.
Related Articles Smaller*Nanodiscs are Suitable for Studying Protein Lipid Interactions by Solution NMR.
Protein J. 2015 May 17;
Authors: Wang X, Mu Z, Li Y, Bi Y, Wang Y
Abstract
Phospholipid bilayer nanodiscs, a newly developed model membrane system, provides "native-like" membrane environment for membrane protein studies. Nanodiscs assembled by membrane scaffold protein and phospholipid bilayer, with defined sizes that can be accurately...
nmrlearner
Journal club
0
05-20-2015 10:27 AM
[NMR paper] Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
Related Articles Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
J Biomol NMR. 2015 Apr;61(3-4):261-74
Authors: Kucharska I, Edrington TC, Liang B, Tamm LK
Abstract
Solution NMR spectroscopy has become a robust method to determine structures and explore the dynamics of integral membrane proteins. The vast majority of previous studies on membrane proteins by solution NMR have been conducted in...
nmrlearner
Journal club
0
04-15-2015 04:40 PM
Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Abstract
Solution NMR spectroscopy has become a robust method to determine structures and explore the dynamics of integral membrane proteins. The vast majority of previous studies on membrane proteins by solution NMR have been conducted in lipid micelles. Contrary to the lipids that form a lipid bilayer in biological membranes, micellar lipids typically contain only a single hydrocarbon chain or two chains that are too short to form a bilayer. Therefore,...
nmrlearner
Journal club
0
02-10-2015 10:56 AM
[NMR paper] Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Related Articles Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Chembiochem. 2014 Apr 1;
Authors: Sušac L, Horst R, Wüthrich K
Abstract
X-ray crystallography and solution NMR of detergent-reconstituted OmpA (outer membrane protein A from E. coli) had shown that this protein forms an eight-stranded transmembrane ?-barrel, but only...
nmrlearner
Journal club
0
04-03-2014 12:59 PM
[NMR paper] Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
Biochim Biophys Acta. 2012 Jun;1818(6):1562-9
Authors: Yu TY, Raschle T, Hiller S, Wagner G
Abstract
Three isoforms of the human voltage-dependent anion channel (VDAC), located...
nmrlearner
Journal club
0
04-04-2013 08:50 PM
[NMR paper] Optimization of the design and preparation of nanoscale phospholipid bilayers for its application to solution NMR.
Optimization of the design and preparation of nanoscale phospholipid bilayers for its application to solution NMR.
Optimization of the design and preparation of nanoscale phospholipid bilayers for its application to solution NMR.
Proteins. 2013 Feb 21;
Authors: Puthenveetil R, Vinogradova O
Abstract
Despite arduous efforts and recent technological developments structural investigation of integral membrane proteins remains a challenge. The primary deterrents include difficulties with their expression, low inherent solubility and various...
nmrlearner
Journal club
0
02-26-2013 06:35 PM
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
Chembiochem. 2010 Sep 24;11(14):1967-70
Authors: Ma P, Mohrlüder J, Schwarten M, Stoldt M, Singh SK, Hartmann R, Pacheco V, Willbold D
nmrlearner
Journal club
0
01-21-2011 01:22 AM
[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
Nanodiscs and Solution NMR: preparation, application and challenges.
Linear Mode
