Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: Proton transfer reactions re studied in all titratable pairs of amino acid side chains where, under physiologically reasonable conditions, one amino acid may function as a donor and the other one as an acceptor. Energy barriers for shifting the proton from donor to acceptor atom re calculated by electronic structure methods at the MP2/6-31++G(d,p) level, and the ll-known double-ll potentials re characterized. The energy difference beten both minima can be expressed by a parabola using as argument the donor-acceptor distance R(DA). In this work, the fit parameters of the quadratic expression are determined for each donor-acceptor pair. Moreover, it was found previously that the energy barriers of the reactions can be expressed by an analytical expression depending on the distance beten donor and acceptor and the energy difference beten donor and acceptor bound states. The validity of this approach is supported by the extensive new data set. This new parameterization of proton transfer barriers beten titratable amino acid side chains allows us to very efficiently estimate proton transfer probabilities in molecular modelling studies or during classical molecular dynamics simulation of biomolecular systems.
['Elena Herzog', 'Tomaso Frigato', 'Volkhard Helms', 'C. Roy D. Lancaster']
I am writing a research paper on a idea Energy barriers of proton transfer reactions between amino acid side chain analogs and water from ab initio calculations.
[{"from": "human", "value": "I am writing a research paper on a idea Energy barriers of proton transfer reactions between amino acid side chain analogs and water from ab initio calculations."}, {"from": "gpt", "value": "Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: Proton transfer reactions re studied in all titratable pairs of amino acid side chains where, under physiologically reasonable conditions, one amino acid may function as a donor and the other one as an acceptor. Energy barriers for shifting the proton from donor to acceptor atom re calculated by electronic structure methods at the MP2/6-31++G(d,p) level, and the ll-known double-ll potentials re characterized. The energy difference beten both minima can be expressed by a parabola using as argument the donor-acceptor distance R(DA). In this work, the fit parameters of the quadratic expression are determined for each donor-acceptor pair. Moreover, it was found previously that the energy barriers of the reactions can be expressed by an analytical expression depending on the distance beten donor and acceptor and the energy difference beten donor and acceptor bound states. The validity of this approach is supported by the extensive new data set. This new parameterization of proton transfer barriers beten titratable amino acid side chains allows us to very efficiently estimate proton transfer probabilities in molecular modelling studies or during classical molecular dynamics simulation of biomolecular systems."}]