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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

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 form...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Updated: Jun 13, 2026

A Practical Guide to Phage- and Robotics-Assisted Near-Continuous Evolution
05:08

A Practical Guide to Phage- and Robotics-Assisted Near-Continuous Evolution

Published on: January 12, 2024

Evolution: a guide to perturb protein function and networks.

Olivier Lichtarge1, Angela Wilkins

  • 1Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA. lichtarge@bcm.edu

Current Opinion in Structural Biology
|May 7, 2010
PubMed
Summary
This summary is machine-generated.

Evolutionary Tracing (ET) identifies functional protein sites by analyzing evolutionary data. This method guides experiments to selectively modify protein interactions, offering a scalable way to perturb cellular networks.

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Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
09:01

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

Published on: March 16, 2011

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A Practical Guide to Phage- and Robotics-Assisted Near-Continuous Evolution
05:08

A Practical Guide to Phage- and Robotics-Assisted Near-Continuous Evolution

Published on: January 12, 2024

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
09:01

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

Published on: March 16, 2011

Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Systems Biology

Background:

  • Protein interaction networks are crucial for cellular functions and disease.
  • Targeting these networks requires selective methods to probe protein interactions.

Purpose of the Study:

  • To introduce Evolutionary Tracing (ET) as a comparative method for identifying functional protein sites.
  • To demonstrate ET's utility in guiding experimental manipulation of protein interactions.

Main Methods:

  • Comparative sequence analysis using Evolutionary Tracing (ET).
  • Identifying functionally important amino acid residues within protein sequences.

Main Results:

  • ET successfully identifies key functional sites in proteins.
  • The method provides a basis for designing experiments to block, recode, or mimic protein interaction determinants.

Conclusions:

  • Evolutionary Tracing offers a scalable approach to perturb specific links within protein networks.
  • This technique has potential applications in understanding and manipulating cellular processes in health and disease.