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Article Dans Une Revue European Journal of Mass Spectrometry Année : 2004

Protonation thermochemistry of alpha-aminoacids bearing a basic residue.

Résumé

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 et 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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