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 07-27-2024, 01:31 PM
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 Micromolar fluoride contamination arising from glass NMR tubes and a simple solution for biomolecular applications

Micromolar fluoride contamination arising from glass NMR tubes and a simple solution for biomolecular applications

Abstract

Fluorine (19F) NMR is emerging as an invaluable analytical technique in chemistry, biochemistry, structural biology, material science, drug discovery, and medicine, especially due to the inherent rarity of naturally occurring fluorine in biological, organic, and inorganic compounds. Here, we revisit the under-reported problem of fluoride leaching from new and unused glass NMR tubes. We characterised the leaching of free fluoride from various types of new and unused glass NMR tubes over the course of several hours and quantify this contaminant to be at micromolar concentrations for typical NMR sample volumes across multiple glass types and brands. We find that this artefact is undetectable for samples prepared in quartz NMR tubes within the timeframes of our experiments. We also observed that pre-soaking new glass NMR tubes combined with rinsing removes this contamination below micromolar levels. Given the increasing popularity of 19F NMR across a wide range of fields, increasing popularity of single-use screening tubes, the long collection times required for relaxation studies and samples of low concentrations, and the importance of avoiding contamination in all NMR experiments, we anticipate that our simple solution will be useful to biomolecular NMR spectroscopists.



Source: Journal of Biomolecular NMR
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Fragment Screening and Fast Micromolar Detection on a Benchtop NMR Spectrometer Boosted by Photoinduced Hyperpolarization
Fragment Screening and Fast Micromolar Detection on a Benchtop NMR Spectrometer Boosted by Photoinduced Hyperpolarization Fragment-based drug design is a well-established strategy for rational drug design, with nuclear magnetic resonance (NMR) on high-field spectrometers as the method of reference for screening and hit validation. However, high-field NMR spectrometers are not only expensive, but require specialized maintenance, dedicated space, and depend on liquid helium cooling which became critical over the recurring global helium shortages. We propose an alternative to high-field NMR...
nmrlearner Journal club 0 08-01-2023 10:34 PM
[NMR paper] Editorial: Biomolecular solid-state NMR: Methods and applications
Editorial: Biomolecular solid-state NMR: Methods and applications No abstract More...
nmrlearner Journal club 0 12-26-2022 06:04 PM
[NMR paper] Applications of high dimensionality experiments to biomolecular NMR.
Applications of high dimensionality experiments to biomolecular NMR. Applications of high dimensionality experiments to biomolecular NMR. Prog Nucl Magn Reson Spectrosc. 2015 Nov;90-91:49-73 Authors: Nowakowski M, Saxena S, Stanek J, ?erko S, Ko?mi?ski W Abstract High dimensionality NMR experiments facilitate resonance assignment and precise determination of spectral parameters such as coupling constants. Sparse non-uniform sampling enables acquisition of experiments of high dimensionality with high resolution in acceptable...
nmrlearner Journal club 0 11-26-2015 12:13 AM
Applications of high dimensionality experiments to biomolecular NMR
Applications of high dimensionality experiments to biomolecular NMR Publication date: Available online 11 July 2015 Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br> Author(s): Micha? Nowakowski , Saurabh Saxena , Jan Stanek , Szymon ?erko , Wiktor Ko?mi?ski</br> High dimensionality NMR experiments facilitate resonance assignment and precise determination of spectral parameters such as coupling constants. Sparse non-uniform sampling enables acquisition of experiments of high dimensionality with high resolution in acceptable time. In this review...
nmrlearner Journal club 0 07-12-2015 07:12 AM
A Simple Device for Cleaning Many NMR Tubes Simultaneously
A Simple Device for Cleaning Many NMR Tubes Simultaneously http://www.spectroscopynow.com/common/images/thumbnails/sepspec19674education.jpgNMR tubes are widely used in organic chemistry. Cleaning a few tubes after use is not a big problem but cleaning hundreds of tubes is a demanding task in terms of time and use of solvents. Here is presented a simple nmr tube cleaner that can clean and dry hundreds of tubes in a short time with minimal exposure of the user to solvents. The tube cleaner is easily assembled from equipment normally present in the organic chemistry laboratory. More...
nmrlearner Educational web pages 0 02-03-2013 09:28 AM
[Question from NMRWiki Q&A forum] Diamagnetic contamination
Diamagnetic contamination How to determine diamagnetic contamination in PRE experiments.In what extent it will effect the Gamma2 values? Check if somebody has answered this question on NMRWiki QA forum
nmrlearner News from other NMR forums 0 12-14-2012 08:57 PM
[NMR paper] An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
An emerging concept of biomolecular dynamics and function: applications of NMR & MRI. Related Articles An emerging concept of biomolecular dynamics and function: applications of NMR & MRI. Magn Reson Med Sci. 2002;1(1):27-31 Authors: Kuwata K A new concept of protein dynamics has emerged quite recently, and a crucial link between protein dynamics and function has been largely established using recent NMR techniques in the solution state. Protein structure is governed by the thermodynamic principle and may not necessarily be unique in the...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Refinement of the NMR solution structure of a protein to remove distortions arising f
Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motion. Related Articles Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motion. Biochemistry. 1991 Apr 23;30(16):3807-11 Authors: Fejzo J, Krezel AM, Westler WM, Macura S, Markley JL The effect of internal motion on the quality of a protein structure derived from nuclear magnetic resonance (NMR) cross relaxation has been investigated experimentally. Internal rotation of the...
nmrlearner Journal club 0 08-21-2010 11:16 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 02:20 PM.


Map