Mass spectrometry study of the sublimation of aliphatic dipeptides

The sublimation of glycyl-L-α-alanine (Gly-Ala), L-α-alanyl-L-α-alanine (Ala-Ala), and DL-α-alanyl-DL-α-valine (Ala-Val) aliphatic dipeptides is studied by electron ionization mass spectrometry in combination with Knudsen effusion. The temperature range in which substances sublime as monomer molecul...

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Published inRussian Journal of Physical Chemistry A Vol. 86; no. 3; pp. 457 - 462
Main Authors Badelin, V. G., Tyunina, E. Yu, Krasnov, A. V., Tyunina, V. V., Giricheva, N. I., Girichev, A. V.
Format Journal Article
LanguageEnglish
Published Dordrecht SP MAIK Nauka/Interperiodica 01.03.2012
Subjects
Chemistry
Chemistry and Materials Science
Physical Chemistry
Physical Chemistry of Surface Phenomena
correlation analysis
mass spectrometry
structural parameters
enthalpy of sublimation
aliphatic dipeptides
amino acids
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Summary:The sublimation of glycyl-L-α-alanine (Gly-Ala), L-α-alanyl-L-α-alanine (Ala-Ala), and DL-α-alanyl-DL-α-valine (Ala-Val) aliphatic dipeptides is studied by electron ionization mass spectrometry in combination with Knudsen effusion. The temperature range in which substances sublime as monomer molecular forms is determined. Enthalpies of sublimation Δ s H °( T ) are determined for Gly-Ala, Ala-Ala, and Ala-Val. It is shown that the enthalpy of sublimation of dipeptides increases with an increase in the side hydrocarbon radical. The unknown Δ s H °(298) values for 17 amino acids and nine dipeptides are estimated using the proposed “structure-property” correlation model, in which the geometry and electron characteristics of molecules are used as structural descriptors.
ISSN:0036-0244
1531-863X
DOI:10.1134/S0036024412030065