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Ionic Bonds00:42

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Overview
When atoms gain or lose electrons to achieve a more stable electron configuration they form ions. Ionic bonds are electrostatic attractions between ions with opposite charges. Ionic compounds are rigid and brittle when solid and may dissociate into their constituent ions in water. Covalent compounds, by contrast, remain intact unless a chemical reaction breaks them.
Opposing Charges Hold Ions Together in Ionic Compounds
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Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
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Sigmatropic rearrangements are a class of pericyclic reactions in which a σ bond migrates from one part of a π system to another. These are intramolecular rearrangements where the total number of σ and π bonds remain unchanged.
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The ionic association is the association of oppositely charged ions in an electrolyte solution to form ion pairs. Bjerrum defined ion pairs as two oppositely charged ions whose electrostatic attraction exceeds the thermal energy of the system, typically expressed as 2kT. Electrostatic attraction depends on ionic charge, separation distance, and the dielectric constant of the medium. Thermal energy, represented by kT, reflects the tendency of ions to move independently due to molecular motion.
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Endothermic ion molecule reactions.

R Orlando1, C Fenselau, R J Cotter

  • 1Structural Biochemistry Center, Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA.

Journal of the American Society for Mass Spectrometry
|November 19, 2013
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Summary
This summary is machine-generated.

This study explores endothermic ion-molecule reactions for biomolecule structural analysis. The technique uses proton transfer to ammonia, enabling peptide sequencing via fragment ions at low energies.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Physical Chemistry

Background:

  • Endothermic ion-molecule reactions are established for determining thermodynamic properties of gaseous ions.
  • Reactive, endothermic collisions are now applied to structural analysis of peptides and biomolecules.

Purpose of the Study:

  • To explore the rationale and origins of using endothermic ion-molecule reactions for biomolecular structural analysis.
  • To detail a novel technique for peptide and biomolecule structural elucidation.

Main Methods:

  • Utilizing endothermic proton transfer reactions involving amide bonds and ammonia.
  • Analyzing dissociation channels opened by additional beam energy.
  • Employing tandem mass spectrometry for ion-molecule reaction studies.

Main Results:

  • The technique relies on proton transfer to ammonia, proceeding through a long-lived collision complex.
  • Additional beam energy activates dissociation channels, producing sequence ions.
  • Spectra comparable to high-energy collision-induced dissociation are achieved at low beam energies.

Conclusions:

  • Endothermic ion-molecule reactions offer a sensitive method for biomolecular structural analysis.
  • The technique allows for peptide sequencing using fragment ions generated at low collision energies.
  • This approach builds upon established ion-molecule reaction studies for novel analytical applications.