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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-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...

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Related Experiment Video

Updated: May 13, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

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Published on: July 25, 2013

Rational-based protein engineering: tips and tools.

Meghna Sobti1, Bridget C Mabbutt

  • 1Structural and Computational Biology Division, Victor Chang Cardiac Research Institute, Sydney, Australia.

Methods in Molecular Biology (Clifton, N.J.)
|March 19, 2013
PubMed
Summary
This summary is machine-generated.

Protein engineering enables the creation of novel biomolecular forms through techniques like site-directed mutagenesis and fusion protein construction. This overview covers strategies for designing and over-expressing recombinant proteins and protein complexes.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Engineering
  • Synthetic Biology

Background:

  • The demand for novel and modified biomolecular forms drives protein engineering.
  • Molecular biology techniques allow for the alteration of protein structure and function.

Purpose of the Study:

  • To provide an overview of protein engineering strategies.
  • To discuss methods for creating mutated, fused, and tagged proteins.
  • To cover the design, over-expression, and assembly of protein complexes.

Main Methods:

  • Site-directed mutagenesis for targeted sequence alteration.
  • Construction of fusion proteins and insertion of affinity tags.
  • Co-expression strategies for engineering protein complexes.

Main Results:

  • Established procedures for altering protein structure and function.
  • Demonstrated methods for generating recombinant proteins and complexes.
  • Highlighted the value of protein complex engineering for bioactive systems.

Conclusions:

  • Rational protein engineering is achievable through established molecular biology techniques.
  • Over-expression and co-expression are key for producing engineered proteins and complexes.
  • Engineered protein complexes offer a route to novel bioactive multicomponent systems.