Thermodynamic characteristics of protolytic equilibria of L-serine in aqueous solutions

Kochergina, L. A.; Volkov, A. V.; Khokhlova, E. A.; Krutova, O. N.

doi:10.1134/s0036024411050177

Cited by 10 publications

(2 citation statements)

References 14 publications

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“…Experimental standard enthalpies (kcal mol À1 ) for the condensation reaction in the gas phase23,[40][41][42][43][44][45] and calculated values from this work…”

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confidence: 99%

Energetics of oxo- and thio-dipeptide formation via amino acid condensation: a systematic computational analysis

Torsello

Orian

Zotti

et al. 2014

Phys. Chem. Chem. Phys.

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Oxo-dipeptides and thio-dipeptides are built via condensation between couples of amino acids and amino thioacids, the latter with the carbonyl oxygen replaced by an sp(2) sulfur. We explored via in silico methods (PBE0/6-31G(d,p) and PBE0/6-311G(d,p)) all the possible combinations and built 800 dipeptides, whose structures were fully optimized. Maps of condensation energies are presented to highlight optimal partners leading to stable dipeptides and critical situations for which lower stability or instability is predicted in terms of Gibbs reaction free energies. To validate the feasibility of our computational investigation, we synthesized and compared the stabilities of two thionated dimers, namely -Gly[Ψ(CSNH)]Gly- and -Phe[Ψ(CSNH)]Phe-, characterized by diverging physico-chemical properties. To the best of our knowledge, this is the first systematic analysis reported for dipeptides built from natural amino acids as well as for their corresponding thio-analogs.

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“…Experimental standard enthalpies (kcal mol À1 ) for the condensation reaction in the gas phase23,[40][41][42][43][44][45] and calculated values from this work…”

mentioning

confidence: 99%

Energetics of oxo- and thio-dipeptide formation via amino acid condensation: a systematic computational analysis

Torsello

Orian

Zotti

et al. 2014

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…Since the characteristics of individual amino acid residues in a protein are due to the nature (physicochemical properties) of the side groups that are present in the hydrated state, the importance of studying the thermodynamic characteristics of amino acids hydration is obvious [9]. To obtain empirical correlations relating the thermodynamic characteristics of interaction between a dissolved substance and a solvent, along with the sizes of the dissolved molecules (which vary in their physicochemical nature), we must acquire a sufficient quantity of experimental data on the enthalpies of solution for amino acids [10][11][12][13][14] and peptides. The latter would allow us to test the additivity of contributions from intermolecular interactions for different groups of molecules.…”

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confidence: 99%