New theoretical methodology for elucidating the solution structure of peptides from NMR data. 3. Solvation effects
Journal Article
·
· Journal of Physical Chemistry
- Florida State Univ., Tallahassee, FL (United States)
A short linear peptide in solution may populate several stable states (denoted here microstates) in thermodynamic equilibrium. Elucidating its dynamic 3D structure by multidimensional nuclear magnetic resonance (NMR) is complex, since the experimentally measured nuclear Overhauser effect intensities (NOEs) represents averages. In previous papers we have developed a new theoretical methodology over the individual contributions based on statistical mechanical considerations for analyzing NMR data from flexible molecules and applied it to Leu-enkephalin(H-Tyr-Gly-Gly-Phe-Leu-OH) using the potential energy function ECEPP. Here we apply this methodology to the same molecule described by the ECEPP energy and a solvation free energy term for water developed by Wesson and Eisenberg. This term is a summation over products of the solvent-accessible surface area of each atom and its solvation parameter. Since water is the most important solvent in biological systems, investigating the properties of this model is an imperative step in the development of our methodology. Thus, the energy barriers of the solvation model are expected to be lower than those of ECEPP alone; hence it is crucial to verify that the MC microstates of the former model are thermodynamically stable and structurally distinctive (i.e., they do not overlap). Criteria for these purposes, proposed in paper 2, are further developed her and applied to the MC microstates. 36 refs., 5 figs., 8 tabs.
- DOE Contract Number:
- FG05-95ER62070
- OSTI ID:
- 237277
- Journal Information:
- Journal of Physical Chemistry, Journal Name: Journal of Physical Chemistry Journal Issue: 12 Vol. 100; ISSN JPCHAX; ISSN 0022-3654
- Country of Publication:
- United States
- Language:
- English
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