Protonation thermochemistry of alpha-aminoacids bearing a basic residue. - Archive ouverte HAL Access content directly
Journal Articles European Journal of Mass Spectrometry Year : 2004

Protonation thermochemistry of alpha-aminoacids bearing a basic residue.

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Abstract

The proton affinity, PA, and protonation entropy, Delta(p)S degree, of glycine (Gly), 1, aspartic acid (Asp), 2, asparagine (Asn), 3, histidine (His), 4, lysine (Lys), 5, glutamic acid (Glu), 6, and glutamine (Gln), 7, have been reinvestigated by the extended kinetic method, using the "isothermal point" method and the orthogonal distance regression, ODR, technique. The proton affinity values of a-aminoacids bearing a basic residue (PA = 926.8; 965.2; 996.0; 993.9; 981.8 and 988.1 kJ.mol(-1) for 2-7, respectively) show significant deviation from the tabulated values. As expected from the effect of a strong intramolecular hydrogen bond in the protonated forms of these peculiar aminoacids, negative protonation entropies are detected (Delta(p)S degree = 36; 43; 37; 29; 95 and 55 J mol(-1) K(-1) for for 27 respectively).
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Dates and versions

hal-00916219 , version 1 (10-12-2013)

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Guy Bouchoux, D.-A. Buisson, Cyril Colas, Michel Sablier. Protonation thermochemistry of alpha-aminoacids bearing a basic residue.. European Journal of Mass Spectrometry, 2004, 10 (6), pp.977-992. ⟨10.1255/ejms.687⟩. ⟨hal-00916219⟩
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