Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Buffers: Overview01:30

Buffers: Overview

5.6K
Buffers play a crucial role in stabilizing the pH of a solution by mitigating the effects of small amounts of added acid or base. They consist of a weak acid and its conjugate base or a weak base and its conjugate acid. A solution of acetic acid and sodium acetate is an example of a buffer that consists of a weak acid and its salt: CH3COOH (aq) + CH3COONa (aq). An example of a buffer that consists of a weak base and its salt is a solution of ammonia and ammonium chloride: NH3 (aq) + NH4Cl (aq).
5.6K
Buffer Effectiveness02:19

Buffer Effectiveness

50.2K
Buffer solutions do not have an unlimited capacity to keep the pH relatively constant . Instead, the ability of a buffer solution to resist changes in pH relies on the presence of appreciable amounts of its conjugate weak acid-base pair. When enough strong acid or base is added to substantially lower the concentration of either member of the buffer pair, the buffering action within the solution is compromised.
The buffer capacity is the amount of acid or base that can be added to a given volume...
50.2K
Buffers: Buffer Capacity01:09

Buffers: Buffer Capacity

1.6K
Buffer capacity is the quantitative measure of a buffer to resist the change in pH. As shown in the following equation, the buffer capacity, denoted by 'beta', is expressed as the number of moles of acid or base needed to change the pH of a one-liter buffer solution by 1 unit. Here, Ca and Cb indicate the number of moles of acid and base, respectively. Note that dpH represents the change in pH.
In the graph, pH is plotted as a function of the number of moles of base (Cb) added to a weak...
1.6K
Bicarbonate-Carbonic Acid Buffer01:22

Bicarbonate-Carbonic Acid Buffer

3.0K
The carbonic acid-bicarbonate buffer system is critical for maintaining the body's pH balance. It operates on the equilibrium:
3.0K
Protein Buffers in Blood Plasma and Cells01:20

Protein Buffers in Blood Plasma and Cells

1.9K
The human body utilizes protein buffer systems to maintain a stable pH. These systems capitalize on the dual role of amino acids, which can act as acids or bases by accepting or releasing hydrogen ions in response to pH changes. Protein buffer systems are particularly significant in the extracellular fluid (ECF) and intracellular fluid (ICF) of active cells, where structural and functional proteins provide substantial buffering capacity.
Certain amino acids can exist in a zwitterion state at a...
1.9K
Polyprotic Acids03:38

Polyprotic Acids

29.5K
Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:
29.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Optimized tRNA structure-seq reveals robust tRNA secondary structures in <i>S. cerevisiae</i> under mild stress conditions.

RNA (New York, N.Y.)·2026
Same author

Nearest Neighbor Parameters for Estimating the Folding Stability of RNA Including Pseudouridine.

bioRxiv : the preprint server for biology·2026
Same author

Increasing the Compositional Heterogeneity of Single-Chain Amphiphile Membranes Supported by Coacervate Cores Alters Stability and Properties of the Hybrid Protocells.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Disordered protein LAT encodes relative levels of signaling pathways in T cell activation.

Science (New York, N.Y.)·2026
Same author

Residue-level mapping of crowding effects on protein phase separation.

Protein science : a publication of the Protein Society·2026
Same author

Optimized tRNA structure-seq reveals robust tRNA secondary structures in <i>S. cerevisiae</i> under mild stress conditions.

bioRxiv : the preprint server for biology·2026
Same journal

The Role of Functional Groups in Substituted Benzoic Acids Used as Dopants in Liquid Crystal Mixtures on the Nematic-Isotropic Transitions.

The journal of physical chemistry. B·2026
Same journal

Hyperfine Coupling Quantifies Hole Delocalization in Triarylamine Radical Cations of D-χ-A Molecules.

The journal of physical chemistry. B·2026
Same journal

A Solvatochromic-Chemometric Framework to Resolve Subtle Polarity Microenvironment Differences in Cycloalkanes Driven by Molecular Conformation and Substituent Effects: A Proof-Of-Concept for Advanced Aviation Fuel Design.

The journal of physical chemistry. B·2026
Same journal

Selective Effects of Backbone Cyclization and Disulfide Bonding as Global Covalent Constraints on the Conformational Ensemble of Sunflower Trypsin Inhibitor-1.

The journal of physical chemistry. B·2026
Same journal

Europium Coordination Structure in Peptide Complexes Resolved with Simulation and X-ray Absorption Spectroscopy.

The journal of physical chemistry. B·2026
Same journal

Competitive Coordination and Structural Evolution of Phenylalanine-Mg<sup>2+</sup> Complexes in Microaqueous Environments: Insights from DFT and Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026
See all related articles

Related Experiment Video

Updated: Sep 12, 2025

Curation of Computational Chemical Libraries Demonstrated with Alpha-Amino Acids
08:21

Curation of Computational Chemical Libraries Demonstrated with Alpha-Amino Acids

Published on: April 13, 2022

2.7K

Primitive Molecular Buffering by Low-Multivalency Coacervates.

Saehyun Choi1, Sindy P Liu1, McCauley O Meyer2,3

  • 1Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.

The Journal of Physical Chemistry. B
|August 7, 2025
PubMed
Summary
This summary is machine-generated.

Coacervate droplets exhibit primitive molecular buffering, maintaining internal composition against environmental changes like salinity and pH. This liquid-liquid phase separation aids early life emergence and has potential applications.

More Related Videos

Author Spotlight: Universal Molecular Retention with 11-Fold Expansion Microscopy
10:31

Author Spotlight: Universal Molecular Retention with 11-Fold Expansion Microscopy

Published on: October 6, 2023

7.7K
On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids
10:32

On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids

Published on: March 2, 2012

24.7K

Related Experiment Videos

Last Updated: Sep 12, 2025

Curation of Computational Chemical Libraries Demonstrated with Alpha-Amino Acids
08:21

Curation of Computational Chemical Libraries Demonstrated with Alpha-Amino Acids

Published on: April 13, 2022

2.7K
Author Spotlight: Universal Molecular Retention with 11-Fold Expansion Microscopy
10:31

Author Spotlight: Universal Molecular Retention with 11-Fold Expansion Microscopy

Published on: October 6, 2023

7.7K
On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids
10:32

On-chip Isotachophoresis for Separation of Ions and Purification of Nucleic Acids

Published on: March 2, 2012

24.7K

Area of Science:

  • Biochemistry
  • Origin of Life Studies
  • Biophysics

Background:

  • Coacervate droplets, formed via liquid-liquid phase separation (LLPS), model intracellular condensates and protocells.
  • Protocells and cells require homeostasis to maintain internal functions against environmental fluctuations (salinity, pH).

Purpose of the Study:

  • To investigate how coacervate molecular composition and RNA compartmentalization are affected by varying salinity and pH.
  • To evaluate the potential of coacervates to provide molecular buffering and resist environmental changes.

Main Methods:

  • Formation and analysis of oligoarginine (R10)/ATP coacervates under diverse salinity and pH conditions.
  • Assessment of coacervate molecular composition and RNA accumulation within droplets.

Main Results:

  • R10/ATP coacervates demonstrated molecular buffering, resisting changes in oligoarginine concentration across different salt conditions.
  • RNA accumulation was observed within coacervates across a range of pH, salinity, and R10/ATP stoichiometry.
  • Salinity influenced molecular buffering and RNA compartmentalization by altering intermolecular binding modes.

Conclusions:

  • LLPS in coacervates provides mechanisms for resisting environmental changes and maintaining molecular availability, mimicking primitive homeostasis.
  • These findings support the role of coacervates in the emergence of life and suggest potential biotechnological applications.