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Related Concept Videos

Diversity of Archaea IV01:29

Diversity of Archaea IV

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Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist...
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Temperature and Thermal Equilibrium01:11

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Heat and temperature are essential concepts for everyone every day. The study of heat and temperature is part of an area of physics known as thermodynamics. It is not always easy to distinguish heat and temperature.
The concept of temperature has evolved from the common concepts of hot and cold. The scientific definition of temperature explains more than just our sense of hot and cold. Temperature is operationally defined as the quantity measured with a thermometer. Furthermore, temperature is...
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Temperature Measurement Sites01:14

Temperature Measurement Sites

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A thermometer measures body temperature. The common sites for measuring body temperature are the oral cavity, axillary region, temporal artery, and skin surface, such as the forehead, abdomen, and axilla. True core body temperature is assessed in the rectum, tympanic membrane, pulmonary artery, esophagus, and urinary bladder.
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Protein Denaturation01:28

Protein Denaturation

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Effects of Temperature on Free Energy

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The spontaneity of a process depends upon the temperature of the system. Phase transitions, for example, will proceed spontaneously in one direction or the other depending upon the temperature of the substance in question. Likewise, some chemical reactions can also exhibit temperature-dependent spontaneities. To illustrate this concept, the equation relating free energy change to the enthalpy and entropy changes for the process is considered:
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Le Chatelier's Principle: Changing Temperature02:19

Le Chatelier's Principle: Changing Temperature

31.0K
Consistent with the law of mass action, an equilibrium stressed by a change in concentration will shift to re-establish equilibrium without any change in the value of the equilibrium constant, K. When an equilibrium shifts in response to a temperature change, however, it is re-established with a different relative composition that exhibits a different value for the equilibrium constant.
To understand this phenomenon, consider the elementary reaction:
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Updated: Oct 7, 2025

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
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Thermometer: a webserver to predict protein thermal stability.

Mattia Miotto1,2, Alexandros Armaos3, Lorenzo Di Rienzo2

  • 1Department of Physics, Sapienza University of Rome, 00185 Rome, Italy.

Bioinformatics (Oxford, England)
|January 12, 2022
PubMed
Summary

Predicting protein thermal stability is challenging. We developed Thermometer, a user-friendly webserver that uses protein structure to assess thermal stability, providing valuable insights for researchers.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Protein thermal properties are crucial for theoretical and practical applications.
  • Accurate prediction of protein thermal stability remains a significant challenge in bioinformatics.

Purpose of the Study:

  • To introduce Thermometer, a novel webserver for predicting protein thermal stability.
  • To provide a publicly available and user-friendly tool for assessing protein thermal stability.

Main Methods:

  • Utilizes protein structural information to predict thermal stability.
  • Implemented as a webserver with an accessible interface.

Main Results:

  • Thermometer is a newly developed webserver.
  • The tool is publicly available and easy to use.

Conclusions:

  • Thermometer offers a solution for predicting protein thermal stability.
  • The webserver facilitates research in protein biophysics and structural biology.