BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 05-20-2014, 11:10 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,028
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default 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 bilayers. One of the key considerations in experimental design is the uniaxial rotational diffusion of the protein that can have a direct influence on the NMR spectral observables. In this regard, temperature plays a fundamental role in modulating the phase properties of the lipids, which directly influences the rotational diffusion rate of the protein in the bilayer. In fact, it is well established that below the main phase transition temperature of the lipid bilayer the protein's motion is significantly slowed while above this critical temperature the rate is increased. In this article, we carried out a systematic comparison of the signal intensity and spectral resolution as a function of temperature using magic-angle-spinning (MAS) solid-state NMR spectroscopy. These observables were directly correlated with the relative fluidity of the lipid bilayer as inferred from differential scanning calorimetry (DSC). We applied our hybrid biophysical approach to polytopic membrane protein multidrug resistance transporters (EmrE and SugE) in the presence of model membrane lipid compositions (DMPC-14:0 and DPPC-16:0). From these experiments, we conclude that the rotational diffusion giving optimal spectral resolution corresponds to a bilayer fluidity of ~5%, which corresponds to the percentage of lipids in the fluid or liquid-crystalline fraction. At the temperature corresponding to this critical value of fluidity, there is sufficient mobility to reduce inhomogeneous line broadening that occurs at lower temperatures. A greater extent of fluidity leads to faster uniaxial rotational diffusion and a sigmoidal-type drop in the NMR signal intensity, which stems from intermediate-exchange dynamics where the motion has a similar frequency as the NMR observables (i.e., dipolar couplings and chemical shift anisotropy). These experiments provide insight into the optimal temperature ranges and corresponding bilayer fluidity to study membrane proteins by solid-state NMR spectroscopy. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.


PMID: 24835018 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
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] Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy. Related Articles Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy. J Biomol NMR. 2013 Dec 4; Authors: Ullrich SJ, Hölper S, Glaubitz C Abstract A considerable limitation of NMR spectroscopy is its inherent low sensitivity. Approximately 90*% of the measuring time is used by the spin system to return to its Boltzmann equilibrium after excitation, which is...
nmrlearner Journal club 0 12-07-2013 01:00 PM
[NMR paper] Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins.
Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins. Related Articles Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins. Prog Nucl Magn Reson Spectrosc. 2013 Nov;75:50-68 Authors: Gopinath T, Mote KR, Veglia G Abstract Oriented solid-state NMR (O-ssNMR) spectroscopy is a major technique for the high-resolution analysis of the structure and topology of transmembrane proteins in native-like environments. Unlike magic angle spinning (MAS)...
nmrlearner Journal club 0 10-29-2013 08:21 PM
[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples. Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples. Nat Protoc. 2013 Nov;8(11):2256-70 Authors: Das N, Murray DT, Cross TA Abstract
nmrlearner Journal club 0 10-27-2013 12:53 AM
[NMR paper] Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein. Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein. Nat Methods. 2013 Sep 8; Authors: Wang S, Munro RA, Shi L, Kawamura I, Okitsu T, Wada A, Kim SY, Jung KH, Brown LS, Ladizhansky V Abstract Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning...
nmrlearner Journal club 0 09-10-2013 08:44 PM
Sensitivity and Resolution Enhancement of Oriented Solid-State NMR: Application to Membrane Proteins
Sensitivity and Resolution Enhancement of Oriented Solid-State NMR: Application to Membrane Proteins Publication date: Available online 12 August 2013 Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br> Author(s): T. Gopinath , Kaustubh R. Mote , Gianluigi Veglia</br> Oriented solid-state NMR (O-ssNMR) spectroscopy is a major technique for the high-resolution analysis of the structure and topology of transmembrane proteins in native-like environments. Unlike magic angle spinning (MAS) techniques, O-ssNMR spectroscopy requires membrane protein...
nmrlearner Journal club 0 08-13-2013 04:09 AM
[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy. Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy. Acc Chem Res. 2013 Jul 5; Authors: Opella SJ Abstract One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
nmrlearner Journal club 0 07-09-2013 02:47 PM
[NMR paper] Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra. J Biomol NMR. 2013 Jan 24; Authors: Emami S, Fan Y, Munro R, Ladizhansky V, Brown LS Abstract One of the biggest challenges in solid-state NMR studies of membrane proteins is to obtain a...
nmrlearner Journal club 0 02-03-2013 10:19 AM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2020, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 03:19 AM.


Map