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  
Old 08-22-2012, 02:13 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,777
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 DEER-Stitch: Combining three- and four-pulse DEER measurements for high sensitivity, deadtime free data

DEER-Stitch: Combining three- and four-pulse DEER measurements for high sensitivity, deadtime free data


Publication year: 2012
Source:Journal of Magnetic Resonance

J.E. Lovett, B.W. Lovett, J. Harmer

Over approximately the last fifteen years the electron paramagnetic resonance (EPR) technique of double electron electron resonance (DEER) has attracted considerable attention since it allows for the precise measurement of the dipole-dipole coupling between radicals and thus can lead to distance information between pairs of radicals separated by up to ca. 8 nm. The “deadtime free” 4-pulse DEER sequence is widely used but can suffer from poor sensitivity if the electron spin-echo decays too quickly to allow collection of a sufficiently long time trace. In this paper we present a method which takes advantage of the much greater sensitivity that the 3-pulse sequence offers over the 4-pulse sequence since the measured electron spin-echo intensity (for equal sequence lengths) is greater. By combining 3- and 4-pulse DEER time traces using a method coined DEER-Stitch (DEERS) accurate dipole-dipole coupling measurements can be made which combine the sensitivity of the 3-pulse DEER sequence with the deadtime free advantage of the 4-pulse DEER sequence. To develop the DEER-Stitch method three systems were measured: a semi-rigid bis-nitroxide labelled nanowire, the bis-nitroxide labelled protein CD55 with a distance between labels of almost 8 nm and a dimeric copper amine oxidase from Arthrobacter globiformis (AGAO).
Graphical abstract

Graphical abstract Highlights

? 2p primary echo in EPR is more intense that 3p refocused echo. ? The echo difference adversely effects 4p DEER compared to 3p DEER. ? 3p and 4p DEER time traces can be combined to give a good-signal-to-noise ratio deadtime free DEERS signal. ? DEERS applied to measure a nanowire, long distances and Cu-Cu coupling.





Source: Journal of Magnetic Resonance
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Orientation selective DEER measurements on vinculin tail at X-band frequencies reveal spin label orientations
Orientation selective DEER measurements on vinculin tail at X-band frequencies reveal spin label orientations Publication year: 2012 Source:Journal of Magnetic Resonance, Volume 216</br> Christoph Abé, Daniel Klose, Franziska Dietrich, Wolfgang H. Ziegler, Yevhen Polyhach, Gunnar Jeschke, Heinz-Jürgen Steinhoff</br> Double electron electron resonance (DEER) spectroscopy has been established as a valuable method to determine distances between spin labels bound to protein molecules. Caused by selective excitation of molecular orientations DEER primary data also...
nmrlearner Journal club 0 03-13-2012 03:33 PM
Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): A study of doubly-spin-labeled T4 lysozyme
Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): A study of doubly-spin-labeled T4 lysozyme Publication year: 2012 Source:Journal of Magnetic Resonance, Volume 216</br> Elka R. Georgieva, Aritro S. Roy, Vladimir M. Grigoryants, Petr P. Borbat, Keith A. Earle, Charles P. Scholes, Jack H. Freed</br> Pulsed dipolar ESR spectroscopy, DEER and DQC, require frozen samples. An important issue in the biological application of this technique is how the freezing rate and concentration of cryoprotectant...
nmrlearner Journal club 0 03-13-2012 03:33 PM
Practical Aspects of High-Sensitivity MultidimensionalC MAS NMR Spectroscopy of Perdeuterated Proteins
Practical Aspects of High-Sensitivity MultidimensionalC MAS NMR Spectroscopy of Perdeuterated Proteins Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 1 March 2012</br> Ümit*Akbey, Barth-Jan*van Rossum, Hartmut*Oschkinat</br> Thedouble nucleus enhanced recoupling(DONER) experiment employs simultaneous irradiation of protons and deuterons to promote spin diffusion processes in a perdeuterated protein. This results in 4-5 times higher sensitivity in 2DC-C correlation experiments as compared to PDSD.Here, a quantitative comparison of PDSD,H-DARR,H-DARR,...
nmrlearner Journal club 0 03-01-2012 11:03 PM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
nmrlearner Journal club 0 02-21-2012 03:40 AM
Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme
Effect of Freezing Conditions on Distances and Their Distributions Derived from Double Electron Electron Resonance (DEER): A Study of Doubly-Spin-Labeled T4 Lysozyme Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 24 January 2012</br> Elka R.*Georgieva, Aritro S.*Roy, Vladimir M.*Grigoryants, Petr P.*Borbat, Keith A.*Earle, ...</br> Pulsed dipolar ESR spectroscopy, DEER and DQC, require frozen samples. An important issue in the biological application of this technique is how the freezing rate and concentration of cryoprotectant could possibly affect the...
nmrlearner Journal club 0 01-25-2012 08:56 AM
Orientation Selective DEER Measurements on Vinculin Tail at X-Band Frequencies Reveal Spin Label Orientations
Orientation Selective DEER Measurements on Vinculin Tail at X-Band Frequencies Reveal Spin Label Orientations Publication year: 2012 Source: Journal of Magnetic Resonance, Available online 8 January 2012</br> Christoph*Abé, Daniel*Klose, Franziska*Dietrich, Wolfgang H.*Ziegler, Yevhen*Polyhach, ...</br> Double electron electron resonance (DEER) spectroscopy has been established as a valuable method to determine distances between spin labels bound to protein molecules. Caused by selective excitation of molecular orientations DEER primary data also depend on the mutual orientation of...
nmrlearner Journal club 0 01-10-2012 03:38 PM
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 March 2011</br> Matthias J.N., Junk , Hans W., Spiess , Dariush, Hinderberger</br> In this study, self-assembled systems of human serum albumin (HSA) and spin-labeled fatty acids are characterized by double electron–electron resonance (DEER). HSA, being the most important transport protein of the human blood, is capable to host up to seven paramagnetic fatty acid...
nmrlearner Journal club 0 03-11-2011 05:00 PM
[NMR paper] High-sensitivity observation of dipolar exchange and NOEs between exchangeable proton
High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy. Related Articles High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy. J Am Chem Soc. 2003 Nov 26;125(47):14222-3 Authors: Paulson EK, Morcombe CR, Gaponenko V, Dancheck B, Byrd RA, Zilm KW A highly sensitive new 1H-detected 3D solid-state NMR method is described for characterizing 1H-1H spin exchange in nanocrystalline samples of...
nmrlearner Journal club 0 11-24-2010 09:16 PM



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 12:44 AM.


Map