Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology
- and others
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.
- Research Organization:
- Los Alamos National Lab., NM (United States)
- Sponsoring Organization:
- USDOE Assistant Secretary for Human Resources and Administration, Washington, DC (United States)
- DOE Contract Number:
- W-7405-ENG-36
- OSTI ID:
- 524859
- Report Number(s):
- LA-UR--97-2321; ON: DE97008596
- Country of Publication:
- United States
- Language:
- English
Similar Records
Human brain mapping: Experimental and computational approaches
Order and correlation contributions to the entropy of hydrophobic solvation
Hydrophobic effects on a molecular scale
Technical Report
·
Sat Oct 31 23:00:00 EST 1998
·
OSTI ID:674923
Order and correlation contributions to the entropy of hydrophobic solvation
Journal Article
·
Sat Mar 21 00:00:00 EDT 2015
· Journal of Chemical Physics
·
OSTI ID:22415529
Hydrophobic effects on a molecular scale
Journal Article
·
Wed Dec 16 23:00:00 EST 1998
· Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical
·
OSTI ID:316053