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Free energy of charges in solvated proteins: microscopic calculations using a reversible charging process
Abstract
Evaluation of the free energy of ionization of acidic groups in proteins may be used as a powerful and general test case for determining the reliability of calculations of electrostatic energies in macromolecules. This work attacks this test case by using an adiabatic charging process that evaluates the changes in free energies associated with ionizing the acidic groups Asp-3 and Glu-7 in bovine pancreatic trypsin inhibitor and aspartic acid in solution. The results of these free energy calculations are very encouraging; the error range is about 1 kcal/mol for these free energy changes of about-70 kcal/mol. This indicates that we are finally approaching the stage of obtaining quantitative results in modeling the energetics of solvated proteins.
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Citations
Cited by
Ion-water interaction potentials derived from free energy perturbation simulations
Ȧqvist, J. (1990) · The Journal of Physical Chemistry · doi:10.1021/j100384a009 · Cited by 1,650
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model
Bashford, D., & Karplus, M. (1990) · Biochemistry · doi:10.1021/bi00496a010 · Cited by 1,083
A Comprehensive Analytical Treatment of Continuum Electrostatics
Schaefer, M., & Karplus, M. (1996) · The Journal of Physical Chemistry · doi:10.1021/jp9521621 · Cited by 561
Toward Theoretical Analyis of Long-Range Proton Transfer Kinetics in Biomolecular Pumps
König, P. H., Ghosh, N., Hoffmann, M., Elstner, M., Tajkhorshid, E., Frauenheim, T., & Cui, Q. (2006) · The Journal of Physical Chemistry A · doi:10.1021/jp052328q · Cited by 114
Metadata
- Authors
- Warshel, A., Sussman, F., & King, G.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1986-12-01
- Volume
- 25
- Issue
- 26
- Pages
- 8368-8372
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1974694453
- Cited by
- 242
- References
- 0
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- closed
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