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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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 Organization01:13

Protein Organization

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Protein Organization01:13

Protein Organization

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Updated: Jun 20, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Understanding protein structure from a percolation perspective.

Dhruba Deb1, Saraswathi Vishveshwara, Smitha Vishveshwara

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

Biophysical Journal
|September 16, 2009
PubMed
Summary
This summary is machine-generated.

Protein structures arise from the interplay of random and selected features in amino acid sequences. Network analysis reveals unique connectivity patterns in protein side-chain interactions, distinct from random models.

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Last Updated: Jun 20, 2026

Protein Crystallization for X-ray Crystallography
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Published on: January 16, 2011

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

  • Protein structure and folding
  • Network science applied to biology
  • Bioinformatics and computational biology

Background:

  • Proteins exhibit vast sequence diversity but limited structural folds.
  • Understanding the principles governing protein structure selection is crucial.

Purpose of the Study:

  • To investigate the role of noncovalent connections in protein structure formation.
  • To analyze the network properties of protein structures at backbone and side-chain levels.

Main Methods:

  • Analysis of noncovalent connections at backbone and side-chain levels.
  • Application of network theory, including bond and clique percolation.
  • Comparison of protein interaction networks with random network models.

Main Results:

  • Protein structure networks exhibit percolation behavior similar to random networks.
  • Side-chain interaction networks show higher connectivity than random networks.
  • Emergent protein structures result from interplay between random and selected features.

Conclusions:

  • Noncovalent interactions and network properties are key to understanding protein structure selection.
  • Protein side-chain networks possess unique characteristics not found in random networks.
  • Amino acid sequences utilize these network features to select specific protein folds.