scholarly journals Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? A comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry

2008 ◽  
Vol 19 (3) ◽  
pp. 332-343 ◽  
Author(s):  
Matthias Conradin Jecklin ◽  
David Touboul ◽  
Cédric Bovet ◽  
Arno Wortmann ◽  
Renato Zenobi
Keyword(s):  
Mass Spectrometry ◽  
Dissociation Constants ◽  
Protein Ligand Interactions ◽  
Ionization Method ◽  
Ligand Interactions

scholarly journals Preliminary investigation of deoxyoligonucleotide binding to ribonuclease A using mass spectrometry: An attempt to develop a lab experience for undergraduates

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 340
Author(s):  
Daniel D. Clark
Keyword(s):  
Mass Spectrometry ◽  
Ion Trap ◽  
Dissociation Constants ◽  
Preliminary Investigation ◽  
Accurate Determination ◽  
Ribonuclease A ◽  
Rnase A ◽  
Protein Ligand Interactions ◽  
Ligand Interactions ◽  
Pancreatic Ribonuclease A

Deoxyoligonucleotide binding to bovine pancreatic ribonuclease A (RNase A) was investigated using electrospray ionization ion-trap mass spectrometry (ESI-IT-MS). Deoxyoligonucleotides included CCCCC (dC5) and CCACC (dC2AC2).  This work was an attempt to develop a biochemistry lab experience that would introduce undergraduates to the use of mass spectrometry for the analysis of protein-ligand interactions.  Titration experiments were performed using a fixed RNase A concentration and variable deoxyoligonucleotide concentrations.  Samples at equilibrium were infused directly into the mass spectrometer under native conditions.  For each deoxyoligonucleotide, mass spectra showed one-to-one binding stoichiometry, with marked increases in the total ion abundance of ligand-bound RNase A complexes as a function of concentration, but the accurate determination of dC5 and dC2AC2 dissociation constants was problematic.

Studies of protein–ligand interactions by NMR

2003 ◽  
Vol 31 (5) ◽  
pp. 1006-1009 ◽  
Author(s):  
J. Clarkson ◽  
I.D. Campbell
Keyword(s):  
Chemical Shift ◽  
Structure Determination ◽  
Dissociation Constants ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Ligand Complex ◽  
Protein Ligand Interactions ◽  
Small Proteins ◽  
Ligand Interactions

Solution-state NMR has become an accepted method for studying the structure of small proteins in solution. This has resulted in over 3000 NMR-based co-ordinate sets being deposited in the Protein Databank. It is becoming increasingly apparent, however, that NMR is also a very powerful tool for accessing interactions between macromolecules and various ligands. These interactions can be assessed at a wide variety of levels, e.g. qualitative screening of libraries of pharmaceuticals and ‘chemical shift mapping’. Dissociation constants can sometimes be obtained in such cases. Another example would be the complete three-dimensional structure determination of a protein–ligand complex. Here we briefly describe a few of the principles involved and illustrate the method with recent examples.

scholarly journals Preliminary investigation of deoxyoligonucleotide binding to ribonuclease A using mass spectrometry: An attempt to develop a lab experience for undergraduates

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 340
Author(s):  
Daniel D. Clark
Keyword(s):  
Mass Spectrometry ◽  
Ion Trap ◽  
Dissociation Constants ◽  
Preliminary Investigation ◽  
Accurate Determination ◽  
Ribonuclease A ◽  
Rnase A ◽  
Protein Ligand Interactions ◽  
Ligand Interactions ◽  
Pancreatic Ribonuclease A

Deoxyoligonucleotide binding to bovine pancreatic ribonuclease A (RNase A) was investigated using electrospray ionization ion-trap mass spectrometry (ESI-IT-MS). Deoxyoligonucleotides included CCCCC (dC5) and CCACC (dC2AC2).  This work was an attempt to develop a biochemistry lab experience that would introduce undergraduates to the use of mass spectrometry for the analysis of protein-ligand interactions.  Titration experiments were performed using a fixed RNase A concentration and variable deoxyoligonucleotide concentrations.  Samples at equilibrium were infused directly into the mass spectrometer under native conditions.  For each deoxyoligonucleotide, mass spectra showed one-to-one binding stoichiometry, with marked increases in the total ion abundance of ligand-bound RNase A complexes as a function of concentration, but the accurate determination of dC5 and dC2AC2 dissociation constants was problematic.

Determination of Pyrantel in Swine Liver by Flame Ionization Gas Chromatography and Confirmation by Gas Chromatography /Mass Spectrometry

1990 ◽  
Vol 73 (6) ◽  
pp. 883-886
Author(s):  
Susan S.C Tai ◽  
Nancy Cargile ◽  
Charlie J Barnes ◽  
Philip Kijak
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Internal Standard ◽  
Gas Chromatography Mass Spectrometry ◽  
Tissue Samples ◽  
Flame Ionization ◽  
Chromatography Mass Spectrometry ◽  
Ionization Method ◽  
Swine Liver

Abstract During an evaluation of the gas chromatography/mass spectrometry (GC/MS) confirmatory procedure of Lynch and Bartoluccl for pyrantel residues in swine tissues, we developed a GC flame Ionization method for quantltatlng pyrantel residues In extracts of swine liver. The method was subjected to trial principally In the laboratories of Biospherics, Inc., using control liver, fortified control liver, and Incurred liver tissue samples. Although the method does not meet all of the current Food and Drug Administration criteria, it compares favorably to the official determinative method. Portions of the same extract can be used for quantitation and for GC/MS confirmation, true recoveries appear to be slightly higher, and an internal standard Is not required. The precision of this method equals or exceeds that of the official determinative method.

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