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Author Wincel, Henryk
Source SpringerLink
Content type Text
Publisher Springer-Verlag
File Format PDF
Copyright Year ©2008
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences
Subject Keyword Analytical Chemistry ♦ Biotechnology ♦ Organic Chemistry ♦ Proteomics ♦ Bioinformatics
Abstract Singly hydrated clusters of deprotonated amino acids were studied using an electrospray high-pressure mass spectrometer equipped with a pulsed ion-beam reaction chamber. Thermochemical data, ΔH $^{ o }$, ΔS $^{ o }$, and ΔG $^{ o }$, for the hydration reaction [AA − H]$^{−}$ + H$_{2}$O = [AA − H]$^{−}$·(H$_{2}$O) were obtained from gas-phase equilibria determinations for AA = Gly, Ala, Val, Pro, Phe, Lys, Met, Trp, Gln, Arg, and Asp. The hydration free-energy changes are found to depend significantly on the side-chain substituents. The water binding energy in [AA − H]$^{−}$·(H$_{2}$O) increases with the gas-phase acidity of AA. The anionic hydrogen bond strengths in [AA − H]$^{−}$·(H$_{2}$O) are compared with those of the cationic bonds in the corresponding AAH$^{+}$·(H$_{2}$O) systems.
ISSN 10440305
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2011-11-22
Publisher Institution The American Society for Mass Spectrometry
Publisher Place New York
e-ISSN 18791123
Journal Journal of The American Society for Mass Spectrometry
Volume Number 19
Issue Number 8
Page Count 7
Starting Page 1091
Ending Page 1097

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Source: SpringerLink