Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

Most enzymes...

Allosteric Proteins-ATCase

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...

Conservation of Protein Domains

Conservation of Protein Domains

You might also read

Related Articles

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

Sort by

Same author

CD98hc-targeted antibody shuttles for central nervous system delivery with broad cross-species reactivity.

Nature biomedical engineering·2026

Same author

Metabolomic Signatures of Brain Atrophy and Ibudilast Response in Progressive Multiple Sclerosis.

medRxiv : the preprint server for health sciences·2026

Same author

Blood Flow Restriction Therapy for the Upper Extremity: An Emerging Adjunct for Patient Recovery and Rehabilitation.

The Orthopedic clinics of North America·2026

Same author

MOCVD Growth of κ‑Ga<sub>2</sub>O<sub>3</sub> on Al-Rich Al <sub><i>x</i></sub> Ga<sub>1-<i>x</i></sub> N Templates: Phase Diagram and Microstructural Evolution.

Crystal growth & design·2026

Same author

Machine learning predictions of IgG1 and IgG4 self-association and high-concentration solution properties.

mAbs·2026

Same author

Proteomic Age Acceleration in Multiple Sclerosis Precedes Symptom Onset and Associates with Severity.

medRxiv : the preprint server for health sciences·2026

Search research articles

Related Experiment Video

Updated: Dec 13, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Directed evolution methods for overcoming trade-offs between protein activity and stability.

Samuel D Stimple^1,2, Matthew D Smith², Peter M Tessier^1,2,3

¹Department of Pharmaceutical Sciences, Biointerfaces Institute, University of Michigan, Ann Arbor, Michigan.

Aiche Journal. American Institute of Chemical Engineers

|July 29, 2020

Summary

This summary is machine-generated.

Directed evolution enhances protein function but often reduces stability. New methods improve understanding and overcome activity/stability trade-offs, enabling highly active and stable engineered proteins for health and environmental applications.

Keywords:

affinity antibody catalysis enzyme protein design protein engineering

More Related Videos

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

Related Experiment Videos

Last Updated: Dec 13, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

Area of Science:

Protein engineering
Biotechnology
Molecular biology

Background:

Engineered proteins are crucial for diverse applications, including enzyme catalysis and therapeutic antibodies.
Directed evolution is a key method for improving protein function through mutagenesis and screening.
Protein stability often decreases as activity is enhanced, limiting directed evolution's success.

Purpose of the Study:

To review advances in understanding protein activity/stability trade-offs.
To highlight innovative methods for overcoming these trade-offs in protein engineering.
To underscore the potential for developing highly active and stable proteins.

Main Methods:

Review of current literature on protein engineering and directed evolution.
Analysis of the origins of activity/stability trade-offs in enzymes and antibodies.
Discussion of experimental and computational strategies to enhance protein stability and activity.

Main Results:

Advances in understanding the molecular basis of activity-stability compromises.
Identification of novel experimental and computational approaches to mitigate these trade-offs.
Demonstration of improved generation of proteins with enhanced activity and stability.

Conclusions:

Overcoming activity/stability trade-offs is critical for advancing protein engineering.
These advances facilitate the development of superior proteins for human health, energy, and environmental solutions.
Future research holds promise for further optimizing engineered protein performance.