Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology
Abstract
This is the final report of a three-year, Laboratory-Directed Research and Development project at the Los Alamos National Laboratory. Hydrophobic effects are central to the structural stability of biomolecules, particularly proteins, in solution but are not understood at a molecular level. This project developed a new theoretical approach to calculation of hydrophobic effects. This information theory approach can be implemented with experimental, including computer simulation-experimental, information. The new theory is consistent with, builds upon, and subsumes previous integral equation and scaled particle statistical thermodynamic modes of hydrophobic effects. the new theory is sufficiently simple to permit application directly to complex biomolecules in solution and to permit further expansion to incorporate more subtle effects.
- Authors:
-
- and others
- Publication Date:
- Research Org.:
- Los Alamos National Lab., NM (United States)
- Sponsoring Org.:
- USDOE Assistant Secretary for Human Resources and Administration, Washington, DC (United States)
- OSTI Identifier:
- 524859
- Report Number(s):
- LA-UR-97-2321
ON: DE97008596
- DOE Contract Number:
- W-7405-ENG-36
- Resource Type:
- Technical Report
- Resource Relation:
- Other Information: PBD: [1997]
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 36 MATERIALS SCIENCE; 55 BIOLOGY AND MEDICINE, BASIC STUDIES; GLASS; SOLVATION; METHANE; PHYSICAL CHEMISTRY; COMPUTERIZED SIMULATION; ANOXIA; MOLECULAR BIOLOGY; ENTROPY; PROTEINS
Citation Formats
Pratt, L.R., Garcia, A.E., and Hummer, G. Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology. United States: N. p., 1997.
Web. doi:10.2172/524859.
Pratt, L.R., Garcia, A.E., & Hummer, G. Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology. United States. doi:10.2172/524859.
Pratt, L.R., Garcia, A.E., and Hummer, G. Fri .
"Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology". United States.
doi:10.2172/524859. https://www.osti.gov/servlets/purl/524859.
@article{osti_524859,
title = {Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology},
author = {Pratt, L.R. and Garcia, A.E. and Hummer, G.},
abstractNote = {This is the final report of a three-year, Laboratory-Directed Research and Development project at the Los Alamos National Laboratory. Hydrophobic effects are central to the structural stability of biomolecules, particularly proteins, in solution but are not understood at a molecular level. This project developed a new theoretical approach to calculation of hydrophobic effects. This information theory approach can be implemented with experimental, including computer simulation-experimental, information. The new theory is consistent with, builds upon, and subsumes previous integral equation and scaled particle statistical thermodynamic modes of hydrophobic effects. the new theory is sufficiently simple to permit application directly to complex biomolecules in solution and to permit further expansion to incorporate more subtle effects.},
doi = {10.2172/524859},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Fri Aug 01 00:00:00 EDT 1997},
month = {Fri Aug 01 00:00:00 EDT 1997}
}