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 11-19-2015, 05:22 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
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 Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies.

Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies.

Related Articles Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies.

J Magn Reson. 2015 Nov 9;261:149-156

Authors: Mote KR, Madhu PK

Abstract
(1)H-detection offers a substitute to the sensitivity-starved experiments often used to characterize biomolecular samples using magic-angle spinning solid-state NMR spectroscopy (MAS-ssNMR). To mitigate the effects of the strong (1)H-(1)H dipolar coupled network that would otherwise severely broaden resonances, high MAS frequencies (>40kHz) are often employed. Here, we have explored the alternative of stroboscopic (1)H-detection at moderate MAS frequencies of 5-30kHz using windowed version of supercycled-phase-modulated Lee-Goldburg homonuclear decoupling. We show that improved resolution in the (1)H dimension, comparable to that obtainable at high spinning frequencies of 40-60kHz without homonuclear decoupling, can be obtained in these experiments for fully protonated proteins. Along with detailed analysis of the performance of the method on the standard tri-peptide f-MLF, experiments on micro-crystalline GB1 and amyloid-? aggregates are used to demonstrate the applicability of these pulse-sequences to challenging biomolecular systems. With only two parameters to optimize, broadbanded performance of the homonuclear decoupling sequence, linear dependence of the chemical-shift scaling factor on resonance offset and a straightforward implementation under experimental conditions currently used for many biomolecular studies (viz. spinning frequencies and radio-frequency amplitudes), we expect these experiments to complement the current (13)C-detection based methods in assignments and characterization through chemical-shift mapping.


PMID: 26580064 [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
Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies
Proton-detected solid-state NMR spectroscopy of fully protonated proteins at slow to moderate magic-angle spinning frequencies Publication date: Available online 9 November 2015 Source:Journal of Magnetic Resonance</br> Author(s): Kaustubh R. Mote, Perunthiruthy K. Madhu</br> 1 H-detection offers a substitute to the sensitivity-starved experiments often used to characterize biomolecular samples using magic-angle spinning solid-state NMR spectroscopy (MAS-ssNMR). To mitigate the effects of the strong 1 H- 1 H dipolar coupled network that...
nmrlearner Journal club 0 11-10-2015 09:10 AM
[NMR paper] Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Solid State Nucl Magn Reson. 2015 Sep 14; Authors: Williams JK, Schmidt-Rohr K, Hong M Abstract The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm,...
nmrlearner Journal club 0 10-07-2015 11:27 AM
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins Publication date: Available online 14 September 2015 Source:Solid State Nuclear Magnetic Resonance</br> Author(s): Jonathan K. Williams, Klaus Schmidt-Rohr, Mei Hong</br> The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped 13C chemical shifts between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet...
nmrlearner Journal club 0 09-14-2015 10:42 PM
Recovery of bulk proton magnetization and sensitivity enhancement in ultrafast magic-angle spinning solid-state NMR
From The DNP-NMR Blog: Recovery of bulk proton magnetization and sensitivity enhancement in ultrafast magic-angle spinning solid-state NMR A large portion of the magnetization in a CP experiment remains unused after an experiment and different strategies exist to make better use of the proton magnetization. Here the authors show their results of testing 7 different cp schemes. Although not directly related to DNP these techniques are still very valuable to increase the sensitivity of an NMR experiment especially in combination with DNP.
nmrlearner News from NMR blogs 0 03-30-2015 06:04 PM
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins Abstract Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of 1H, 13C, and 15N resonances and structural analysis in fully protonated proteins. We demonstrate that 13C detected 3D experiments are highly efficient and permit assignments of the majority of backbone resonances, as shown in an 89-residue dynein light chain 8, LC8 protein. With these experiments, we...
nmrlearner Journal club 0 11-11-2014 11:57 AM
[NMR paper] Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.
Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins. Related Articles Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins. J Biomol NMR. 2014 Nov 9; Authors: Guo C, Hou G, Lu X, O'Hare B, Struppe J, Polenova T Abstract Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of (1)H, (13)C, and (15)N...
nmrlearner Journal club 0 11-10-2014 10:59 PM
[NMR paper] Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. J Am Chem Soc. 2014 Aug 7; Authors: Barbet-Massin E, Pell AJ, Retel J, Andreas LB, Jaudzems K, Franks WT, Nieuwkoop AJ, Hiller M, Higman VA, Guerry P, Bertarello A, Knight MJ, Felletti M, Le Marchand T, Kotelovica S, Akopjana I, Tars K, Stoppini M, Bellotti V, Bolognesi M, Ricagno S, Chou JJ, Griffin RG, Oschkinat H, Lesage A, Emsley L, Herrmann T, Pintacuda G Abstract ...
nmrlearner Journal club 0 08-08-2014 01:45 PM
[NMR paper] High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning. Related Articles High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning. J Biomol NMR. 2013 Dec 13; Authors: Ward ME, Wang S, Krishnamurthy S, Hutchins H, Fey M, Brown LS, Ladizhansky V Abstract Magic angle spinning nuclear magnetic resonance (MAS NMR) is well suited for the study of membrane proteins in membrane mimetic and native membrane...
nmrlearner Journal club 0 12-18-2013 04:00 PM


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 - 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 03:35 PM.


Map