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Related Concept Videos

Entropy02:39

Entropy

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Salt particles that have dissolved in water never spontaneously come back together in solution to reform solid particles. Moreover, a gas that has expanded in a vacuum remains dispersed and never spontaneously reassembles. The unidirectional nature of these phenomena is the result of a thermodynamic state function called entropy (S). Entropy is the measure of the extent to which the energy is dispersed throughout a system, or in other words, it is proportional to the degree of disorder of a...
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The first law of thermodynamics is quantitatively formulated via an equation relating the internal energy of a system, the heat exchanged by it, and the work done on it. A quantitative formulation of the second law of thermodynamics leads to defining a state function, the entropy.
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The process of surrounding a solute with solvent is called solvation. It involves evenly distributing the solute within the solvent. The rule of thumb for determining a solvent for a given compound is that like dissolves like. A good solvent has molecular characteristics similar to those of the compound to be dissolved. For example, polar solutions dissolve polar solutes, and apolar solvents dissolve apolar solutes. A polar solvent is a solvent that has a high dielectric constant (ϵ...
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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...
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Entropy and the Second Law of Thermodynamics01:20

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The second law of thermodynamics can be stated quantitatively using the concept of entropy. Entropy is the measure of disorder of the system.
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Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
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Local entropy in proteins.

Patrick Senet1, Adrien Guzzo2, Patrice Delarue1

  • 1Laboratoire Interdisciplinaire Carnot de Bourgogne ICB, UMR 6303, Université Bourgogne Europe, CNRS F-21000 Dijon France psenet@ube.fr +33 (0)3 80396132 +33 (0)3 80396130.

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|January 26, 2026
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Summary
This summary is machine-generated.

We developed a local entropy metric to quantify protein structural complexity. This method reveals how temperature and mutations alter protein dynamics and conformational ensembles.

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Area of Science:

  • Protein dynamics and structural biology
  • Computational biophysics

Background:

  • Proteins exist as dynamic ensembles, but how temperature and mutations affect these ensembles is not well understood.
  • Existing methods for measuring protein fluctuations have limitations.

Purpose of the Study:

  • To introduce a novel local entropy metric for quantifying protein structural complexity.
  • To investigate the impact of temperature and mutations on protein conformational ensembles.

Main Methods:

  • Developed a local entropy metric based on Shannon entropy and graph-derived accessible substates.
  • Utilized molecular dynamics simulations for the gpW protein and alpha-synuclein.
  • Analyzed residue-specific entropy curves and compared them with other fluctuation measures.

Main Results:

  • Local entropy shows a sharp transition near the melting point for the gpW protein.
  • Residue-specific entropy reveals distinct unfolding patterns dependent on spatial scale.
  • Local entropy captures unique features distinct from accessible volume and packing entropy.
  • Parkinson's disease mutations in alpha-synuclein reduce local entropy and perturb distant regions.

Conclusions:

  • Local entropy provides a continuous measure of structural complexity across various protein states.
  • This metric captures the remodeling of conformational ensembles by temperature and mutations.
  • Local entropy correlates with NMR observables and offers a generalizable framework for quantifying protein disorder.