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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
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: Jun 30, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Protein-protein interaction and quaternary structure.

Joël Janin1, Ranjit P Bahadur, Pinak Chakrabarti

  • 1Yeast Structural Genomics, IBBMC UMR 8619 CNRS, Université Paris-Sud, Orsay, France. joel.janin@u-psud.fr

Quarterly Reviews of Biophysics
|September 25, 2008
PubMed
Summary

Specific protein interactions are crucial for cellular processes and molecular assembly. Computational methods reveal that biologically significant protein interfaces are tightly packed, unlike those in protein crystals, providing a basis for recognition.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Protein-protein interactions are fundamental to cellular structure and function.
  • These interactions stabilize macromolecular assemblies like oligomeric proteins and viral capsids.
  • Understanding these interactions is key to deciphering biological processes.

Purpose of the Study:

  • To present structure-based computational methods for analyzing protein-protein interfaces.
  • To characterize the quaternary structure of protein assemblies.
  • To analyze the properties and structural basis of subunit interfaces.

Main Methods:

  • Utilized structure-based computational approaches.
  • Analyzed size, composition, and atomic packing of subunit interfaces.
  • Compared interfaces across various biological assemblies (oligomeric proteins, viral capsids, protein-nucleic acid complexes).

Main Results:

  • Biologically significant protein interfaces are generally close-packed.
  • Non-specific interfaces in protein crystals are loosely packed, distinguishing specific recognition.
  • Interfaces have distinct core and rim regions with differing amino acid compositions and conservation.

Conclusions:

  • Close packing of interfaces provides a structural basis for specific protein recognition.
  • The core-rim distinction aids in correlating structural data with experimental findings (mutagenesis, self-assembly).
  • These findings enhance understanding of macromolecular assembly and protein function.