Actions for (Simulations of biomolecular dynamics) [electronic resource].
(Simulations of biomolecular dynamics) [electronic resource].
- Published
- Washington, D.C : United States. Dept. of Energy. Office of Energy Research, 1990.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy. - Physical Description
- Pages: (3 pages) : digital, PDF file
- Additional Creators
- Harvard University, United States. Department of Energy. Office of Energy Research, and United States. Department of Energy. Office of Scientific and Technical Information
Access Online
- Restrictions on Access
- Free-to-read Unrestricted online access
- Summary
- The basic objective of the research supported by the Department of Energy grant has been to increase our understanding of and predictive ability for macromolecular systems (proteins, nucleic acids, etc.) of biological interest. For this purpose a wide range of large-scale simulations were made. They are concerned with equilibrium and non-equilibrium phenomena on time scales of up to a nanosecond for isolated macromolecules and macromolecules in solution. As a result of such simulations, a fundamental increase in our knowledge of the dynamical and thermodynamic properties and functions of such macromolecules, as well as more complex assemblies of biological interest has been achieved. Of particular interest are simulations of protein folding and the prediction of structural and thermodynamic changes in proteins and protein-liganded interactions induced by site-directed mutagenesis. Recent advances in computational techniques, including simulation methods for free energy changes, have been used for determining how to modify existing proteins to introduce altered properties. A molecular dynamics simulation method has been used for determining the contributions of individual amino acid residues and solvent molecules to free energy changes in proteins. A method was developed for protein secondary structure prediction based a neural network and molecular dynamics simulations were used to calculate in incoherent neutron scattering spectra of myoglobin.
- Report Numbers
- E 1.99:doe/er/60543-3
doe/er/60543-3 - Subject(s)
- Other Subject(s)
- Note
- Published through SciTech Connect.
01/01/1990.
"doe/er/60543-3"
"DE91001977" - Funding Information
- FG02-87ER60543
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