Solid state NMR and protein–protein interactions in membranes

		BioNMR > Educational resources > Journal club
Solid state NMR and protein–protein interactions in membranes

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

09-11-2013, 09:15 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

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

Solid state NMR and protein–protein interactions in membranes

Solid state NMR and protein–protein interactions in membranes

Publication date: Available online 11 September 2013
Source:Current Opinion in Structural Biology

Author(s): Yimin Miao , Timothy A Cross

Solid state NMR spectroscopy has evolved rapidly in recent years into an excellent tool for the characterization of membrane proteins and their complexes. In the past few years it has also become clear that the structure of membrane proteins, especially helical membrane proteins is determined, in part, by the membrane environment. Therefore, the modeling of this environment by a liquid crystalline lipid bilayer for solid state NMR has generated a unique tool for the characterization of native conformational states, local and global dynamics, and high-resolution structure for these proteins. Protein–protein interactions can also benefit from this solid state NMR capability to characterize membrane proteins in a native-like environment. These complexes take the form of oligomeric structures and hetero-protein interactions both with water-soluble proteins and other membrane proteins.

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein. Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein. Related Articles Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein. J Mol Biol. 2013 Apr 11; Authors: Leftin A, Job C, Beyer K, Brown MF Abstract Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson's disease. It is...	nmrlearner	Journal club	0	04-16-2013 07:46 PM
Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein Publication date: Available online 11 April 2013 Source:Journal of Molecular Biology</br> Author(s): Avigdor Leftin , Constantin Job , Klaus Beyer , Michael F. Brown</br> Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson’s disease. It is well established that membrane binding is initiated at the N-terminus of the protein and...	nmrlearner	Journal club	0	04-11-2013 09:27 PM
[NMR paper] Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study. Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study. Related Articles Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study. Biochim Biophys Acta. 2013 Apr 5; Authors: Ciesielski F, Griffin DC, Rittig M, Moriyón I, Bonev BB Abstract Lipopolysaccharide (LPS) is a major component of the external leaflet of bacterial outer membranes, key pro-inflammatory factor and an important mediator of host-pathogen interactions. In host cells it activates the complement...	nmrlearner	Journal club	0	04-10-2013 07:21 PM
[NMR paper] Solid-state NMR approaches to study protein structure and protein-lipid interactions. Solid-state NMR approaches to study protein structure and protein-lipid interactions. Solid-state NMR approaches to study protein structure and protein-lipid interactions. Methods Mol Biol. 2013;974:357-87 Authors: Aisenbrey C, Michalek M, Salnikov ES, Bechinger B Abstract Solid-state NMR spectroscopy has been developed for the investigation of membrane-associated polypeptides and remains one of the few techniques to reveal high-resolution structural information in liquid-disordered phospholipid bilayers. In particular, oriented samples...	nmrlearner	Journal club	0	02-14-2013 02:37 PM
Protein Interactions In Membranes - Chemical & Engineering News Protein Interactions In Membranes - Chemical & Engineering News http://nt2.ggpht.com/news/tbn/EsMJPExWlLTDnM/6.jpg Chemical & Engineering News <img alt="" height="1" width="1" /> Protein Interactions In Membranes Chemical & Engineering News When researchers use NMR to study protein-complex formation in cell-membrane mimics called micelles, they run the risk of misinterpreting shifts in the spectra. For instance, protein A and protein B might just appear to be associating because the ...	nmrlearner	Online News	0	11-29-2011 04:49 AM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif Journal of the American Chemical Society DOI: 10.1021/ja204062v http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw	nmrlearner	Journal club	0	07-27-2011 11:24 AM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR. In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR. In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR. J Am Chem Soc. 2011 Jul 21; Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...	nmrlearner	Journal club	0	07-23-2011 08:54 AM
[NMR paper] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy. Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy. J Am Chem Soc. 2003 Nov 5;125(44):13336-7 Authors: Lesage A, Böckmann A Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...	nmrlearner	Journal club	0	11-24-2010 09:16 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