Related Experiment Video

Updated: Aug 12, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

[Thermally-induced changes in structure-kinetic properties of lactate dehydrogenase]

V G Artiukhov, M A Nakvasina, V V Popova

    Biofizika
    |July 1, 1994
    PubMed

    More Related Videos

    Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue06:18

    Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue

    Published on: June 21, 2018

    Measuring Enzymatic Stability by Isothermal Titration Calorimetry08:37

    Measuring Enzymatic Stability by Isothermal Titration Calorimetry

    Published on: March 26, 2019

    Related Concept Videos

    Effects of Temperature on Free Energy02:11

    Effects of Temperature on Free Energy

    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:
    Introduction to Mechanisms of Enzyme Catalysis01:13

    Introduction to Mechanisms of Enzyme Catalysis

    For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
    Loss of Carboxy Group as CO2: Decarboxylation of β-Ketoacids01:02

    Loss of Carboxy Group as CO2: Decarboxylation of β-Ketoacids

    Carboxylic acids, upon heating, undergo a decarboxylation reaction by releasing carbon dioxide gas. Monocarboxylic acids do not undergo decarboxylation easily. However, a silver salt of carboxylic acid reacts with bromine or iodine under high temperature to release carbon dioxide gas and forms halide with one less carbon. This reaction is called the Hunsdiecker reaction.
    Regioselective Formation of Enolates01:33

    Regioselective Formation of Enolates

    As depicted in the figure below, the unsymmetrical ketones can form two possible enolates: less substituted or more substituted enolates. Usually, the thermodynamic enolates are formed from the more substituted α-carbon atom, while the kinetic enolates are formed faster by deprotonation from the less substituted position. The thermodynamic enolates have lower energy, so they are more stable. But the energy required to form kinetic enolates is less.
    Loss of Carboxy Group as CO2: Decarboxylation of Malonic Acid Derivatives01:35

    Loss of Carboxy Group as CO2: Decarboxylation of Malonic Acid Derivatives

    Just like β-keto acids—which upon thermal decarboxylation form ketones—β-dicarboxylic acids undergo decarboxylation to generate monocarboxylic acids with the liberation of carbon dioxide.
    Protein Denaturation01:28

    Protein Denaturation

    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...