A theoretical analysis on hydration thermodynamics of proteins
- PMID: 16848615
- DOI: 10.1063/1.2213980
A theoretical analysis on hydration thermodynamics of proteins
Abstract
The hydration free energy (HFE) of several proteins modeled using the all-atom force field is calculated by employing the three-dimensional reference interaction site model theory, a recently developed integral equation theory of molecular solvation. The HFE is decomposed into the energetic and entropic components under the isochoric condition. The former comprises the protein-water interaction energy and the water reorganization energy arising from the structural changes induced in water. Each component is further decomposed into the nonelectrostatic and electrostatic contributions. It is found that the HFE is governed by the nonelectrostatic hydration entropy and the electrostatic hydration energy. The nonelectrostatic hydration entropy is almost exclusively ascribed to the translational entropy loss of water upon the protein insertion. It asymptotically becomes proportional to the excluded volume (EV) for water molecules as the protein size increases. The hydration energy is determined by the protein-water interaction energy which is half compensated by the water reorganization energy. These energy terms are approximately proportional to the water-accessible surface area (ASA). The energetic and entropic contributions are balanced with each other and the HFE has no apparent linear relation with the EV and ASA.
Similar articles
-
Theoretical analysis on changes in thermodynamic quantities upon protein folding: essential role of hydration.J Chem Phys. 2007 Jun 14;126(22):225102. doi: 10.1063/1.2743962. J Chem Phys. 2007. PMID: 17581082
-
Crucial importance of translational entropy of water in pressure denaturation of proteins.J Chem Phys. 2006 Jul 14;125(2):24910. doi: 10.1063/1.2217011. J Chem Phys. 2006. PMID: 16848614
-
Partial molar volume of proteins studied by the three-dimensional reference interaction site model theory.J Phys Chem B. 2005 Apr 14;109(14):6658-65. doi: 10.1021/jp045667c. J Phys Chem B. 2005. PMID: 16851748
-
Unraveling water's entropic mysteries: a unified view of nonpolar, polar, and ionic hydration.Acc Chem Res. 2008 Aug;41(8):957-67. doi: 10.1021/ar7001478. Acc Chem Res. 2008. PMID: 18710198 Review.
-
Continuum molecular electrostatics, salt effects, and counterion binding--a review of the Poisson-Boltzmann theory and its modifications.Biopolymers. 2008 Feb;89(2):93-113. doi: 10.1002/bip.20877. Biopolymers. 2008. PMID: 17969016 Review.
Cited by
-
Atomic-level thermodynamics analysis of the binding free energy of SARS-CoV-2 neutralizing antibodies.Proteins. 2023 May;91(5):694-704. doi: 10.1002/prot.26458. Epub 2023 Jan 1. Proteins. 2023. PMID: 36564921 Free PMC article.
-
Total free energy analysis of fully hydrated proteins.Proteins. 2023 Jan;91(1):74-90. doi: 10.1002/prot.26411. Epub 2022 Aug 25. Proteins. 2023. PMID: 35964252 Free PMC article.
-
Mutation-induced change in chignolin stability from π-turn to α-turn.RSC Adv. 2020 Jun 15;10(38):22797-22808. doi: 10.1039/d0ra01148g. eCollection 2020 Jun 10. RSC Adv. 2020. PMID: 35514567 Free PMC article.
-
Local environment effects on charged mutations for developing aggregation-resistant monoclonal antibodies.Sci Rep. 2020 Dec 3;10(1):21191. doi: 10.1038/s41598-020-78136-1. Sci Rep. 2020. PMID: 33273506 Free PMC article.
-
Effect of linker on the binding free energy of stapled p53/HDM2 complex.PLoS One. 2020 Apr 30;15(4):e0232613. doi: 10.1371/journal.pone.0232613. eCollection 2020. PLoS One. 2020. PMID: 32353067 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
