Counterion condensation as saturation effect under the influence of ion hydration.

Biophys Chem

Institute of Medical Physics and Biophysics, University of Leipzig, Germany.

Published: May 2001

Polyelectrolyte solutions are often described by structural theories. These theories in some cases yield values for the counterion concentration at the charged monomer surface that exceed the saturation concentration. This means a change of the ion properties due to ion immobilization or ion condensation in close vicinity to the polymer chain. The extent of this counterion condensation (CIC) and the respective surface potential are calculated from the saturation concentrations of the electrolyte involved including the influence of ion hydration on the effective dielectric number. In this paper, we shall consider all these influences by a fundamental differential equation and a set of explicit formulae yielding quantitative expressions without linearization. All calculations are based on the abstraction of an idealized elementary cell.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0301-4622(01)00148-xDOI Listing

Publication Analysis

Top Keywords

counterion condensation
8
influence ion
8
ion hydration
8
ion
5
condensation saturation
4
saturation influence
4
hydration polyelectrolyte
4
polyelectrolyte solutions
4
solutions described
4
described structural
4

Similar Publications

We theoretically investigate how the intranuclear environment influences the charge of a nucleosome core particle (NCP)-the fundamental unit of chromatin consisting of DNA wrapped around a core of histone proteins. The molecular-based theory explicitly considers the size, shape, conformation, charge, and chemical state of all molecular species-thereby linking the structural state with the chemical/charged state of the system. We investigate how variations in monovalent and divalent salt concentrations, as well as pH, affect the charge distribution across different regions of an NCP and quantify the impact of charge regulation.

View Article and Find Full Text PDF

Balancing Group 1 Monoatomic Ion-Polar Compound Interactions in the Polarizable Drude Force Field: Application in Protein and Nucleic Acid Systems.

J Phys Chem B

December 2024

University of Maryland Computer-Aided Drug Design Center, Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201, United States.

An accurate force field (FF) is the foundation of reliable results from molecular dynamics (MD) simulations. In our recently published work, we developed a protocol to generate atom pair-specific Lennard-Jones (known as NBFIX in CHARMM) and through-space Thole dipole screening (NBTHOLE) parameters in the context of the Drude polarizable FF based on readily accessible quantum mechanical (QM) data to fit condensed phase experimental thermodynamic benchmarks, including the osmotic pressure, diffusion coefficient, ionic conductivity, and solvation free energy, when available. In the present work, the developed protocol is applied to generate NBFIX and NBTHOLE parameters for interactions between monatomic ions (specifically Li, Na, K, Rb, Cs, and Cl) and common functional groups found in proteins and nucleic acids.

View Article and Find Full Text PDF
Article Synopsis
  • Sulfated cyclodextrins are negatively charged molecules used in capillary electrophoresis for separating chiral compounds, but their effective charge can be lower than expected due to counterion binding.
  • This study used capillary isotachophoresis and capillary zone electrophoresis to measure the effective charge numbers and ionic mobilities of two types of sulfated cyclodextrins: single isomer and randomly highly sulfated.
  • Results showed that while the effective charge numbers of single isomer sulfated cyclodextrins closely matched their sulfate groups, the randomly highly sulfated versions had their effective charges reduced by 22.2%-27.8%, leading to lower ionic mobilities for the single isomer
View Article and Find Full Text PDF

We theoretically investigate how the intranuclear environment influences the charge of a nucleosome core particle (NCP) - the fundamental unit of chromatin consisting of DNA wrapped around a core of histone proteins. The molecular-based theory explicitly considers the size, shape, conformations, charges, and chemical states of all molecular species - thereby linking the structural state with the chemical/charged state of the system. We investigate how variations in monovalent and divalent salt concentrations, as well as pH, affect the charge distribution across different regions of an NCP and quantify the impact of charge regulation.

View Article and Find Full Text PDF

Driving Forces in the Formation of Biocondensates of Highly Charged Proteins: A Thermodynamic Analysis of the Binary Complex Formation.

Biomolecules

November 2024

Institut für Chemie und Biochemie, Freie Universität Berlin, Forschungsbau SupraFab, Altensteinstrasse 23a, 14195 Berlin, Germany.

Article Synopsis
  • The study focuses on the interaction between the positively charged linker histone H1 and the negatively charged chaperone prothymosin α (ProTα), highlighting their strong binding in physiological conditions.
  • The analysis employs a thermodynamic model that considers the influence of counterion release and hydration on the complex formation.
  • The findings reveal that the binding energy is primarily driven by the release of counterions from ProTα, while changes in water interactions and conformational constraints contribute to a significant negative change in free energy.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!