Affiliation:
1. Laboratoire des Mécanismes Réactionnels, UMR 7651, Ecole Polytechnique, 91128 Palaiseau cedex, France
2. CEN Saclay, 91190 Gif sur Yvette cedex, France
Abstract
The proton affinity ( PA) and protonation entropy, ΔpS°, 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 technique. The proton affinity values of α-amino acids 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 amino acids, negative protonation entropies are detected (ΔpS° = −36, −43, −37, −29, −95 and −55 J mol−1 K−1 for 2–7, respectively).
Subject
Spectroscopy,Atomic and Molecular Physics, and Optics,General Medicine
Cited by
39 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献