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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...

Conservation of Protein Domains

Conservation of Protein Domains

Structural Protein Function

Structural Protein Function

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...

Protein Families

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...

Protein Families

Protein Families

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Updated: Mar 20, 2026

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

Evolution-Based Functional Decomposition of Proteins.

Olivier Rivoire¹, Kimberly A Reynolds², Rama Ranganathan³

¹Laboratoire Interdisciplinaire de Physique, CNRS and Université Grenoble Alpes, Grenoble, France.

Plos Computational Biology

|June 3, 2016

Summary

This summary is machine-generated.

Statistical coupling analysis (SCA) reveals protein sectors, which are networks of coevolving amino acids. This evolution-based method helps understand protein function and adaptation, with new tools provided for analysis.

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Last Updated: Mar 20, 2026

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

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Published on: July 14, 2015

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

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Published on: July 16, 2017

Area of Science:

Protein bioinformatics
Computational biology
Molecular evolution

Background:

Protein function arises from amino acid interaction patterns.
Statistical coupling analysis (SCA) studies amino acid coevolution in protein families.
SCA identifies functional units called sectors.

Purpose of the Study:

To present the principles and practice of SCA.
To introduce new methods for sector analysis.
To provide a Python-based software package (pySCA) for SCA.

Main Methods:

Statistical coupling analysis (SCA) of amino acid coevolution.
Analysis of protein sequence ensembles.
Development of the pySCA software package.

Main Results:

SCA identifies sectors as coupled networks of amino acids.
Sector amino acid interactions correlate with functional lineage divergence.
pySCA facilitates sector analysis.

Conclusions:

Sectors represent a fundamental unit of protein function and adaptation.
SCA provides insights into the structural basis of protein function.
The pySCA package offers new tools for protein research.