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Related Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
Kinetic Energy for a Rigid Body01:13

Kinetic Energy for a Rigid Body

Imagine a solid object involved in a general planar movement, with its center of mass pinpointed at a spot labeled G. The object's kinetic energy relative to an arbitrary point A can be quantified for each of its particles - the ith particle in this case. This measurement is achieved through the employment of the relative velocity definition. The position vector, known as rA, extends from point A to the mass element i.
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...

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Updated: Jun 15, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Protein kinetic stability.

Jose M Sanchez-Ruiz1

  • 1Departamento de Quimica Fisica, Universidad de Granada, 18071-Granada, Spain. sanchezr@ugr.es

Biophysical Chemistry
|March 5, 2010
PubMed
Summary
This summary is machine-generated.

Protein kinetic stability, a crucial barrier against denaturation, ensures function over time. This review highlights its importance in evolution, cellular environments, and biotechnology, contrasting with thermodynamic stability research.

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Last Updated: Jun 15, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Protein stability is vital for biological function and evolution.
  • Two types exist: thermodynamic stability (equilibrium) and kinetic stability (barrier-mediated).
  • Kinetic stability protects proteins in harsh environments and aids evolution and biotechnology.

Purpose of the Study:

  • To review experimental evidence for widespread protein kinetic stabilization.
  • To discuss the role of natural selection in kinetic stability.
  • To explore mechanisms of kinetic stability and its link to diseases.

Main Methods:

  • Review of experimental data on protein kinetic stability.
  • Discussion of evolutionary and mechanistic aspects.
  • Analysis of kinetic destabilization in protein misfolding diseases.

Main Results:

  • Kinetic stability is widespread and crucial for protein function under physiological conditions.
  • Natural selection likely favors proteins with sufficient kinetic stability.
  • Mechanisms for kinetic stability involve high energy barriers preventing unfolding.
  • Kinetic destabilization is linked to protein misfolding diseases.

Conclusions:

  • Kinetic stability is a critical, often overlooked, aspect of protein function and evolution.
  • Further research into kinetic stability is essential for understanding biology and disease.
  • Biotechnological applications can benefit from understanding and engineering kinetic stability.