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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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 09-22-2010, 05:27 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,175
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 Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phosph

Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.

Related Articles Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.

J Magn Reson. 2010 Aug 24;

Authors: Chu S, Maltsev S, Emwas AH, Lorigan GA

A new approach for determining the membrane immersion depth of a spin-labeled probe has been developed using paramagnetic relaxation enhancement (PRE) in solid-state NMR spectroscopy. A DOXYL spin label was placed at different sites of 1-palmitoyl-2-stearoyl-sn-glycero-3-phosphocholine (PSPC) phospholipid bilayers as paramagnetic moieties and the resulting enhancements of the longitudinal relaxation (T(1)) times of (31)P nuclei on the surface of the bilayers were measured by a standard inversion recovery pulse sequence. The (31)P NMR spin-lattice relaxation times decrease steadily as the DOXYL spin label moves closer to the surface as well as the concentration of the spin-labeled lipids increase. The enhanced relaxation vs. the position and concentration of spin-labels indicate that PRE induced by the DOXYL spin label are significant to determine longer distances over the whole range of the membrane depths. When these data were combined with estimated correlation times Ï?(c), the r(-6)-weighted, time-averaged distances between the spin-labels and the (31)P nuclei on the membrane surface were estimated. The application of using this solid-state NMR PRE approach coupled with site-directed spin labeling (SDSL) may be a powerful method for measuring membrane protein immersion depth.

PMID: 20851650 [PubMed - as supplied by publisher]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
nmrlearner Journal club 0 10-21-2011 10:04 PM
Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen
Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen Abstract In studies of membrane proteins, knowledge of protein topology can provide useful insight into both structure and function. In this work, we present a solution NMR method for the measurement the tilt angle and average immersion depth of alpha helices in membrane proteins, from analysis of the paramagnetic relaxation rate enhancements arising from dissolved oxygen. No modification to the micelle or protein is necessary, and the topology of both transmembrane and...
nmrlearner Journal club 0 09-30-2011 08:01 PM
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement. Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement. J Phys Chem Lett. 2011 Jul 21;2(14):1836-1841 Authors: Tang M, Berthold DA, Rienstra CM Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is...
nmrlearner Journal club 0 08-16-2011 01:19 PM
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR Abstract Magic-angle spinning solid-state NMR measurements of 15N longitudinal paramagnetic relaxation enhancements (PREs) in 13C,15N-labeled proteins modified with Cu2+-chelating tags can yield multiple long-range electron-nucleus distance restraints up to ~20 Ã? (Nadaud et al. in J Am Chem Soc 131:8108â??8120, 2009). Using the EDTA-Cu2+ K28C mutant of B1 immunoglobulin...
nmrlearner Journal club 0 08-13-2011 02:47 AM
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR.
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of (15)N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. J Biomol NMR. 2011 Aug 9; Authors: Nadaud PS, Sengupta I, Helmus JJ, Jaroniec CP Magic-angle spinning solid-state NMR...
nmrlearner Journal club 0 08-10-2011 12:30 PM
[NMR paper] PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic p
PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins. Related Articles PASE (PAramagnetic signals enhancement): a new method for NMR study of paramagnetic proteins. J Magn Reson. 1998 Sep;134(1):154-7 Authors: Bondon A, Mouro C A new method for NMR spectra acquisition of paramagnetic proteins is described, based on the simple use of homonuclear broadband decoupling of the diamagnetic region. Several advantages are associated with this method which was applied to one-dimensional spectra, to 1D...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[Question from NMRWiki Q&A forum] Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NM
Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NMR I am a beginner in NMR spectroscopy and I would like to learn more about relaxation editing experiments vs PRE. A colleague of mine is doing the 13C CP-MAS NMR experim. and he using cellulose II powder, regenerated cellulose and milled reg cellulose. We are interested in C4 resonance of cellulose II, good resolved resonance, to better understand the supramolecular structure of cellulose II. As experiments: long relaxation experiments - PRE with aqueous CuSO4 solution of certain concentration, does the...
nmrlearner News from other NMR forums 0 10-15-2010 05:16 PM
[Question from NMRWiki Q&A forum] Does anyone know something about paramagnetic relaxation enhancement (PRE)?
Does anyone know something about paramagnetic relaxation enhancement (PRE)? Does anyone know something about paramagnetic relaxation enhancement (PRE)? i would like to try this method on my cellulose materials. What info can you take out of it? Thank you very much. Check if somebody has answered this question on NMRWiki QA forum
nmrlearner News from other NMR forums 0 09-08-2010 12:08 AM



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 - 2024, 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 06:44 AM.


Map