NMR paper Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

		BioNMR > Educational resources > Journal club
[NMR paper] Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

01-31-2015, 04:16 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

Related Articles Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

J Biomol NMR. 2015 Jan 30;

Authors: Eddy MT, Su Y, Silvers R, Andreas L, Clark L, Wagner G, Pintacuda G, Emsley L, Griffin RG

Abstract
The human voltage dependent anion channel 1 (VDAC) is a 32*kDa ?-barrel integral membrane protein that controls the transport of ions across the outer mitochondrial membrane. Despite the determination of VDAC solution and diffraction structures, a structural basis for the mechanism of its function is not yet fully understood. Biophysical studies suggest VDAC requires a lipid bilayer to achieve full function, motivating the need for atomic resolution structural information of VDAC in a membrane environment. Here we report an essential step toward that goal: extensive assignments of backbone and side chain resonances for VDAC in DMPC lipid bilayers via magic angle spinning nuclear magnetic resonance (MAS NMR). VDAC reconstituted into DMPC lipid bilayers spontaneously forms two-dimensional lipid crystals, showing remarkable spectral resolution (0.5-0.3*ppm for (13)C line widths and

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR Abstract The human voltage dependent anion channel 1 (VDAC) is a 32Â*kDa Î²-barrel integral membrane protein that controls the transport of ions across the outer mitochondrial membrane. Despite the determination of VDAC solution and diffraction structures, a structural basis for the mechanism of its function is not yet fully understood. Biophysical studies suggest VDAC requires a lipid bilayer to achieve full function, motivating the need...	nmrlearner	Journal club	0	01-30-2015 12:15 PM
[NMR paper] Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation. Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation. Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation. J Biomol NMR. 2015 Jan 13; Authors: Ding Y, Fujimoto LM, Yao Y, Marassi FM Abstract Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the...	nmrlearner	Journal club	0	01-13-2015 02:31 PM
Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation Abstract Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the need for sample crystallization or precipitation (Bertini et al. Proc Natl Acad Sci USA 108(26):10396â??10399, 2011). Inspired by the potential benefits of this method, we have investigated the ability to sediment lipid bilayer...	nmrlearner	Journal club	0	01-12-2015 11:31 PM
[NMR paper] Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy. Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy. Related Articles Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy. Biochim Biophys Acta. 2014 May 13; Authors: Banigan JR, Gayen A, Traaseth NJ Abstract Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid...	nmrlearner	Journal club	0	05-20-2014 11:10 PM
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy Publication date: Available online 13 May 2014 Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br> Author(s): James R. Banigan , Anindita Gayen , Nathaniel J. Traaseth</br> Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid bilayers. One of the key considerations in experimental design is the uniaxial rotational...	nmrlearner	Journal club	0	05-14-2014 04:50 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
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...	nmrlearner	Journal club	0	10-10-2011 06:27 AM
[NMR paper] Lipid-protein interactions in DHPC micelles containing the integral membrane protein Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Related Articles Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13533-7 Authors: Fernández C, Hilty C, Wider G, Wüthrich K Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed...	nmrlearner	Journal club	0	11-24-2010 08:58 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off