Identifying lipids tightly bound to an integral membrane protein - ScienceDirect.com

		BioNMR > NMR community > Online News
Identifying lipids tightly bound to an integral membrane protein - ScienceDirect.com

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

06-04-2024, 05:01 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,778

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

Identifying lipids tightly bound to an integral membrane protein - ScienceDirect.com

Identifying lipids tightly bound to an integral membrane protein - ScienceDirect.com

Identifying lipids tightly bound to an integral membrane protein ScienceDirect.com Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids - ScienceDirect.com Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids - ScienceDirect.com Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids ScienceDirect.com Read here	nmrlearner	Online News	0	05-19-2024 04:30 AM
Solution NMR investigations of integral membrane proteins: Challenges and innovations - ScienceDirect.com Solution NMR investigations of integral membrane proteins: Challenges and innovations - ScienceDirect.com Solution NMR investigations of integral membrane proteins: Challenges and innovations ScienceDirect.com Read here	nmrlearner	Online News	0	05-14-2024 05:29 AM
Probing amino acid side chains of the integral membrane protein PagP by solution NMR: Side chain immobilization ... - ScienceDirect Probing amino acid side chains of the integral membrane protein PagP by solution NMR: Side chain immobilization ... - ScienceDirect Probing amino acid side chains of the integral membrane protein PagP by solution NMR: Side chain immobilization ... ScienceDirect Read here	nmrlearner	Online News	0	01-27-2024 01:53 PM
[NMR paper] 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	nmrlearner	Journal club	0	01-31-2015 04:16 PM
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
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA. Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA. Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA. J Am Chem Soc. 2011 Mar 1; Authors: Renault M, Bos MP, Tommassen J, Baldus M Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...	nmrlearner	Journal club	0	03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif Journal of the American Chemical Society DOI: 10.1021/ja109469c http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I	nmrlearner	Journal club	0	03-02-2011 02:01 AM
[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...	nmrlearner	Journal club	0	12-01-2010 06:56 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