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

What is Genetic Engineering?00:49

What is Genetic Engineering?

80.2K
Overview
80.2K
Heat Engines01:10

Heat Engines

3.7K
A heat engine is a device used to extract heat from a source and then convert it into mechanical work used for various applications. For example, a steam engine on an old-style train can produce the work needed for driving the train.
Whenever we consider heat engines (and associated devices such as refrigerators and heat pumps), we do not use the standard sign convention for heat and work. For convenience, we assume that the symbols Qh, Qc, and W represent only the amounts of heat transferred...
3.7K
Internal Combustion Engine01:20

Internal Combustion Engine

2.7K
The internal combustion engine is a heat engine that uses the byproducts of combustion as the working fluid instead of using a heat transfer medium to transfer heat. The combustion is done in a way that produces high-pressure combustion products that can be expanded through a turbine or piston to create work. Internal combustion engines can again be categorized into three kinds: (1) spark ignition gasoline engines, most commonly used in automobiles, (2) compression ignition diesel engines that...
2.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.7K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Protein and Protein Structure02:15

Protein and Protein Structure

87.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.6K
Protein Complex Assembly02:41

Protein Complex Assembly

16.8K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.8K

You might also read

Related Articles

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

Sort by
Same author

Mechanistic Elucidation and Stereochemical Consequences of Alternative Binding of Alkenyl Substrates by Engineered Arylmalonate Decarboxylase.

Journal of the American Chemical Society·2025
Same author

Designing Efficient Enzymes: Eight Predicted Mutations Convert a Hydroxynitrile Lyase into an Efficient Esterase.

bioRxiv : the preprint server for biology·2023
Same author

Identifying Key Residues in Lysine Decarboxylase for Soluble Expression Using Consensus Design Soluble Mutant Screening (ConsenSing).

ACS synthetic biology·2023
Same author

Enzymatic Enantioselective anti-Markovnikov Hydration of Aryl Alkenes.

Angewandte Chemie (International ed. in English)·2022
Same author

Toward advanced ionic liquids. Polar, enzyme-friendly solvents for biocatalysis.

Biotechnology and bioprocess engineering : BBE·2021
Same author

High-Level Production of Lysine in the Yeast Saccharomyces cerevisiae by Rational Design of Homocitrate Synthase.

Applied and environmental microbiology·2021
Same journal

Fluorescent merocyanines: from fundamental properties to applications as molecular probes, in bioimaging and as emissive dye aggregates.

Chemical Society reviews·2026
Same journal

Direct impure water electrolysis at industrial scale.

Chemical Society reviews·2026
Same journal

Catalytic valorization of polyolefins: from catalysts and processes to reactors.

Chemical Society reviews·2026
Same journal

Designing stable π-radicals.

Chemical Society reviews·2026
Same journal

Antibacterial drug discovery: challenges and preclinical promises from synthetic small molecules.

Chemical Society reviews·2026
Same journal

Selective carbon-carbon bond cleavage involving alkene moieties.

Chemical Society reviews·2026
See all related articles

Related Experiment Video

Updated: Feb 4, 2026

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells
09:20

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells

Published on: July 6, 2021

2.8K

Engineering more stable proteins.

Romas Kazlauskas1

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 174 Gortner Lab., 1479 Gortner Avenue, St Paul, Minnesota, USA.

Chemical Society Reviews
|October 12, 2018
PubMed
Summary
This summary is machine-generated.

Protein stability is crucial for function but proteins often unfold. This study explores engineering more stable proteins by identifying stabilizing amino acid substitutions using web-based tools.

More Related Videos

Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

15.0K
Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

3.6K

Related Experiment Videos

Last Updated: Feb 4, 2026

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells
09:20

Reliably Engineering and Controlling Stable Optogenetic Gene Circuits in Mammalian Cells

Published on: July 6, 2021

2.8K
Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

15.0K
Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

3.6K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Protein function depends on a stable, folded conformation, which is inherently unstable and prone to unfolding into a flexible, unstructured state.
  • Protein folding is driven by hydrophobic interactions and hydrogen bonding, while unfolding is favored by increased backbone conformational freedom.
  • Protein stability is typically assessed by measuring reversible unfolding induced by heat or chemical denaturants like urea.

Purpose of the Study:

  • To provide a tutorial on utilizing web-based tools for identifying amino acid substitutions that enhance protein stability.
  • To guide researchers in engineering more stable proteins by shifting the folding-unfolding equilibrium towards the folded state.

Main Methods:

  • Focus on web-based computational tools for predicting stabilizing mutations.
  • Discuss strategies for stabilizing the folded conformation or destabilizing the unfolded ensemble.
  • Mention common methods for measuring protein stability, such as thermal or chemical denaturation.

Main Results:

  • The tutorial emphasizes practical application of bioinformatics tools for protein stabilization.
  • Identifies key principles in protein engineering for enhancing stability through targeted amino acid substitutions.

Conclusions:

  • Engineering protein stability is achievable through strategic amino acid substitutions.
  • Web-based tools offer efficient methods for identifying mutations that confer enhanced protein stability.
  • Beyond unfolding, other instability factors like chemical modification and aggregation must also be considered in protein engineering.