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

Second Law of Thermodynamics02:49

Second Law of Thermodynamics

25.5K
In the quest to identify a property that may reliably predict the spontaneity of a process, a promising candidate has been identified: entropy. Processes that involve an increase in entropy of the system (ΔS > 0) are very often spontaneous; however, examples to the contrary are plentiful. By expanding consideration of entropy changes to include the surroundings, a significant conclusion regarding the relation between this property and spontaneity may be reached. In thermodynamic models, the...
25.5K
Second Law of Thermodynamics00:53

Second Law of Thermodynamics

66.0K
The Second Law of Thermodynamics states that entropy, or the amount of disorder in a system, increases each time energy is transferred or transformed. Each energy transfer results in a certain amount of energy that is lost—usually in the form of heat—that increases the disorder of the surroundings. This can also be demonstrated in a classic food web. Herbivores harvest chemical energy from plants and release heat and carbon dioxide into the environment. Carnivores harvest the...
66.0K
Gibbs Free Energy02:39

Gibbs Free Energy

36.1K
One of the challenges of using the second law of thermodynamics to determine if a process is spontaneous is that it requires measurements of the entropy change for the system and the entropy change for the surroundings. An alternative approach involving a new thermodynamic property defined in terms of system properties only was introduced in the late nineteenth century by American mathematician Josiah Willard Gibbs. This new property is called the Gibbs free energy (G) (or simply the free...
36.1K
Entropy within the Cell01:22

Entropy within the Cell

12.2K
A living cell's primary tasks of obtaining, transforming, and using energy to do work may seem simple. However, the second law of thermodynamics explains why these tasks are harder than they appear. None of the energy transfers in the universe are completely efficient. In every energy transfer, some amount of energy is lost in a form that is unusable. In most cases, this form is heat energy. Thermodynamically, heat energy is defined as the energy transferred from one system to another that...
12.2K
The Second Law of Thermodynamics01:14

The Second Law of Thermodynamics

6.2K
In the quest to identify a property that may reliably predict the spontaneity of a process, a promising candidate has been identified: entropy. Scientists refer to the measure of randomness or disorder within a system as entropy. High entropy means high disorder and low energy. To better understand entropy, think of a student’s bedroom. If no energy or work were put into it, the room would quickly become messy. It would exist in a very disordered state, one of high entropy. Energy must be...
6.2K
Uncertainty: Overview00:59

Uncertainty: Overview

1.2K
In analytical chemistry, we often perform repetitive measurements to detect and minimize inaccuracies caused by both determinate and indeterminate errors. Despite the cares we take, the presence of random errors means that repeated measurements almost never have exactly the same magnitude. The collective difference between these measurements - observed values - and the estimated or expected value is called uncertainty. Uncertainty is conventionally written after the estimated or expected value.
1.2K

You might also read

Related Articles

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

Sort by
Same author

Polymer brush-induced depletion interactions and clustering of membrane proteins.

The Journal of chemical physics·2021
Same author

Water-mediated biomolecular dynamics and allostery.

The Journal of chemical physics·2020
Same author

From octopus to dendrite-Semiflexible polyelectrolyte brush condensates in trivalent counterion solution.

The Journal of chemical physics·2018
See all related articles

Related Experiment Video

Updated: Nov 9, 2025

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
10:02

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Published on: February 18, 2014

9.2K

Thermodynamic uncertainty relation to assess biological processes.

Yonghyun Song1, Changbong Hyeon1

  • 1Korea Institute for Advanced Study, Seoul 02455, South Korea.

The Journal of Chemical Physics
|April 9, 2021
PubMed
Summary

This study explores how biological processes balance speed, precision, and energy cost using the thermodynamic uncertainty relation (TUR). The TUR sets a universal bound on how efficiently these processes can operate. The researchers found that some biological systems, like molecular motors and gene regulation, work close to this theoretical limit. However, enzymatic processes are suboptimal when substrate concentration is at the Michaelis constant. The study also shows how biological copying processes balance precision with error rates. The findings suggest that biological systems are evolved to optimize conflicting requirements, such as minimizing energy use while maintaining accuracy.

Keywords:
thermodynamic uncertainty relationbiological process efficiencymolecular motor mechanicsenzymatic process precision

Frequently Asked Questions

More Related Videos

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.2K
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

39.7K

Related Experiment Videos

Last Updated: Nov 9, 2025

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection
10:02

Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

Published on: February 18, 2014

9.2K
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.2K
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

39.7K

Area of Science:

  • Biophysics of cellular processes
  • Thermodynamics in biological systems
  • Molecular motor mechanics

Background:

Biological systems operate far from equilibrium, balancing speed, precision, and energy cost. Prior research has shown that enzymatic and motor processes involve inherent fluctuations. It was already known that these fluctuations relate to thermodynamic costs. However, the exact relationship between these variables remains unclear. No prior work had resolved how biological systems approach theoretical bounds on efficiency. This gap motivated the exploration of the thermodynamic uncertainty relation (TUR). The TUR provides a universal bound on the trade-off between precision and energy dissipation. Understanding how biological processes approach this bound is essential for assessing their optimality. This paper addresses that uncertainty by analyzing TUR in various biological contexts.

Purpose Of The Study:

The study aims to evaluate how biological processes approach the thermodynamic uncertainty relation (TUR) bound. It focuses on the trade-offs between speed, fluctuations, and energy cost in nonequilibrium systems. The authors seek to determine whether biological systems operate close to or far from the TUR limit. They examine enzymatic processes, molecular motors, and information transfer mechanisms. The specific problem involves quantifying the uncertainty product Q as a measure of process precision. The motivation comes from observing suboptimal Q values at the Michaelis constant. The researchers propose that biological systems may work around these suboptimal conditions. This analysis helps assess the evolutionary optimization of biological functions.

Main Methods:

The researchers reviewed literature on biological processes governed by the thermodynamic uncertainty relation (TUR). They calculated the uncertainty product Q for enzymatic and motor processes. They compared Q values with the theoretical TUR bound to assess process precision. The study included molecular motors and biomass-producing systems as case studies. They analyzed how Q relates to the error rate in information transfer processes. The researchers also examined gene regulation and chaperone-assisted protein folding. They synthesized findings from various biological systems into a unified framework. The approach involved comparing theoretical predictions with empirical observations.

Main Results:

The uncertainty product Q was found to be suboptimal when substrate concentration equals the Michaelis constant. Some biological processes avoid this suboptimal condition. Molecular motors and biomass-producing systems approach the TUR bound closely. For biomass production, the Q value reflects a balance between precision and error rate. The study found that gene regulation and protein folding also exhibit trade-offs. These processes minimize errors while maintaining thermodynamic efficiency. The TUR bound serves as a reference for evaluating biological optimality. The results suggest that biological systems are evolved to balance conflicting requirements.

Conclusions:

The authors suggest that biological systems approach the thermodynamic uncertainty relation (TUR) bound. They propose that processes like gene regulation and protein folding minimize errors while maintaining efficiency. The study highlights how biological systems balance precision, speed, and energy cost. The uncertainty product Q serves as a useful metric for assessing process optimality. The findings suggest that biological systems are evolved to work around suboptimal conditions. The TUR provides a universal framework for evaluating biological processes. The researchers propose that this analysis helps understand evolutionary optimization. They suggest that further studies could explore other biological systems using the TUR framework.

The TUR measures the trade-off between process precision and thermodynamic cost using the uncertainty product Q.

At the Michaelis constant, enzymatic processes exhibit suboptimal Q values, suggesting a trade-off between precision and energy cost.

Molecular motors operate close to the TUR bound, indicating a balance between speed, fluctuations, and energy dissipation.

Q quantifies the balance between process precision and error rate in biological copying processes like DNA replication.

Gene regulation and chaperone-assisted protein folding minimize errors while maintaining thermodynamic efficiency.

The study suggests biological systems are evolved to balance conflicting functional requirements, such as precision and energy cost.