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 10-31-2022, 04:08 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 Combined H-N Cross-Polarization and Carbonyl Detection NMR Spectroscopy Allow to Record High-Resolution, High-Sensitivity Spectra of Alpha-Synuclein in Bacterial Cells

Combined H-N Cross-Polarization and Carbonyl Detection NMR Spectroscopy Allow to Record High-Resolution, High-Sensitivity Spectra of Alpha-Synuclein in Bacterial Cells

Studies of intrinsically disordered proteins (IDPs) under physiological conditions by conventional NMR methods based on proton detection are severely limited by fast proton amide solvent exchange. Carbon detection has been proposed as a solution to the exchange problem but is hampered by low sensitivity. Here, we present a protocol combining proton-nitrogen cross-polarization and carbonyl detection to record high-resolution and high-sensitivity NMR spectra of IDPs under physiological conditions....

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Erratum to: Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR.
Erratum to: Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR. Related Articles Erratum to: Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR. J Biomol NMR. 2017 Dec 11;: Authors: Takeuchi K, Arthanari H, Shimada I, Wagner G Abstract The authors regret a mistake appeared in the supplement of this paper.
nmrlearner Journal club 0 12-13-2017 06:15 PM
Erratum to: Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR
Erratum to: Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR Abstract The authors regret a mistake appeared in the supplement of this paper. Source: Journal of Biomolecular NMR
nmrlearner Journal club 0 12-11-2017 12:45 PM
High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe
High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe Abstract Field-dependent NMR studies of bio-molecular systems using a sample shuttling hardware operating on a high-field NMR apparatus have provided valuable structural and dynamic information. We have recently published a design of a compact sample transportation device, called â??field-cyclerâ??, which was installed in a commercial spectrometer and which provided highly precise positioning and stability during high speed...
nmrlearner Journal club 0 11-19-2016 08:35 PM
[NMR paper] Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy. Related Articles Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy. Angew Chem Int Ed Engl. 2016 May 9; Authors: Lopez J, Schneider R, Cantrelle FX, Huvent I, Lippens G Abstract Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based...
nmrlearner Journal club 0 05-10-2016 04:13 PM
[NMR paper] Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR.
Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR. Related Articles Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR. J Biomol NMR. 2015 Oct 23; Authors: Takeuchi K, Arthanari H, Shimada I, Wagner G Abstract Detection of (15)N in multidimensional NMR experiments of proteins has sparsely been utilized because of the low gyromagnetic ratio (?) of nitrogen and the presumed low sensitivity of such experiments. Here we show that selecting the TROSY...
nmrlearner Journal club 0 10-27-2015 12:33 PM
Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR
Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR Abstract Detection of 15N in multidimensional NMR experiments of proteins has sparsely been utilized because of the low gyromagnetic ratio (γ) of nitrogen and the presumed low sensitivity of such experiments. Here we show that selecting the TROSY components of proton-attached 15N nuclei (TROSY 15NH) yields high quality spectra in high field magnets (>600Â*MHz) by taking advantage of the slow 15N transverse relaxation and compensating for the inherently low...
nmrlearner Journal club 0 10-24-2015 05:49 AM
Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes
Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes Abstract Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of 1JHC scalar couplings and limited chemical shift...
nmrlearner Journal club 0 06-19-2014 10:21 PM
TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra
TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra Abstract While NMR studies of proteins typically aim at structure, dynamics or interactions, resonance assignments represent in almost all cases the initial step of the analysis. With increasing complexity of the NMR spectra, for example due to decreasing extent of ordered structure, this task often becomes both difficult and time-consuming, and the recording of high-dimensional data with high-resolution may be essential. Random sampling of the evolution time space,...
nmrlearner Journal club 0 07-20-2012 11:13 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 05:40 AM.


Map