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

Go Back   BioNMR > NMR community > News from NMR blogs
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 03-21-2020, 12:53 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 Prediction of flow effects in quantitative NMR measurements #DNPNMR

From The DNP-NMR Blog:

Prediction of flow effects in quantitative NMR measurements #DNPNMR

Friebel, Anne, Thomas Specht, Erik von Harbou, Kerstin Münnemann, and Hans Hasse. “Prediction of Flow Effects in Quantitative NMR Measurements.” Journal of Magnetic Resonance 312 (March 2020): 106683.


https://doi.org/10.1016/j.jmr.2020.106683.


A method for the prediction of the magnetization in flow NMR experiments is presented, which can be applied to mixtures. It enables a quantitative evaluation of NMR spectra of flowing liquid samples even in cases in which the magnetization is limited by the flow. A transport model of the nuclei’s magnetization, which is based on the Bloch-equations, is introduced into a computational fluid dynamics (CFD) code. This code predicts the velocity field and relative magnetization of different nuclei for any chosen flow cell geometry, fluid and flow rate. The prediction of relative magnetization is used to correct the observed reduction of signal intensity caused by incomplete premagnetization in fast flowing liquids. By means of the model, quantitative NMR measurements at high flow rates are possible. The method is predictive and enables calculating correction factors for any flow cell design and operating condition based on simple static T1 time measurements. This makes time-consuming calibration measurements for assessing the influence of flow effects obsolete, which otherwise would have to be carried out for each studied condition. The new method is especially interesting for flow measurements with compact medium field NMR spectrometers, which have small premagnetization volumes. In the present work, experiments with three different flow cells in a medium field NMR spectrometer were carried out. Acetonitrile, water, and mixtures of these components were used as model fluids. The experimental results for the magnetization were compared to the predictions from the CFD model and good agreement was observed.




Go to The DNP-NMR Blog for more info.
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
A highly versatile automatized setup for quantitative measurements of PHIP enhancements #SABRE #NMR
From The DNP-NMR Blog: A highly versatile automatized setup for quantitative measurements of PHIP enhancements #SABRE #NMR p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica} Kiryutin, A.S., et al., A highly versatile automatized setup for quantitative measurements of PHIP enhancements. J. Magn. Reson., 2017. 285: p. 26-36. https://www.ncbi.nlm.nih.gov/pubmed/29073504
nmrlearner News from NMR blogs 0 02-02-2018 11:31 PM
[NMR paper] Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy.
Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy. Related Articles Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy. J Phys Chem Lett. 2017 Nov 17;: Authors: Mukhopadhyay D, Nadaud PS, Shannon MD, Jaroniec CP Abstract We demonstrate rapid quantitative measurements of site-resolved paramagnetic relaxation enhancements (PREs), which are a...
nmrlearner Journal club 0 11-19-2017 05:41 AM
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins Abstract Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ?/? torsion angles seen in intrinsically disordered proteins (IDPs). The ?/? torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and 3JHN-H? coupling constants for a...
nmrlearner Journal club 0 10-25-2017 10:14 PM
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins Abstract Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ?/? torsion angles seen in intrinsically disordered proteins (IDPs). The ?/? torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and 3JHN-H? coupling constants for a...
nmrlearner Journal club 0 09-08-2017 12:52 PM
Quantitative Effects of O-Linked Glycans onProtein Folding
Quantitative Effects of O-Linked Glycans onProtein Folding http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00483/20170815/images/medium/bi-2017-00483e_0007.gif Biochemistry DOI: 10.1021/acs.biochem.7b00483 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/wJNjqab3y6M More...
nmrlearner Journal club 0 08-16-2017 08:53 AM
Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization
From The DNP-NMR Blog: Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization Miclet E, Abergel D, Bornet A, Milani J, Jannin S, Bodenhausen G. Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization. The Journal of Physical Chemistry Letters. 2014;5(19):3290-5. http://dx.doi.org/10.1021/jz501411d
nmrlearner News from NMR blogs 0 06-03-2015 11:04 PM
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
nmrlearner Journal club 0 12-05-2011 04:07 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 Off
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 06:38 AM.


Map