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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...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Evolutionary Relationships through Genome Comparisons02:54

Evolutionary Relationships through Genome Comparisons

Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...

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Related Experiment Video

Updated: Jun 19, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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

Published on: July 14, 2015

Exploratory visual analysis of conserved domains on multiple sequence alignments.

T J Jankun-Kelly1, Andrew D Lindeman, Susan M Bridges

  • 1Institute for Digital Biology and Department of Computer Science and Engineering, Bagley College of Engineering, Mississippi State University, Mississippi, USA. tjk@acm.org

BMC Bioinformatics
|October 9, 2009
PubMed
Summary
This summary is machine-generated.

MSAVis visually displays protein sequence alignments and conserved domains simultaneously using color and brightness. This tool helps biologists efficiently analyze protein conservation and function across multiple species.

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

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Related Experiment Videos

Last Updated: Jun 19, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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Published on: July 14, 2015

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Published on: February 10, 2023

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:

  • Bioinformatics
  • Computational Biology
  • Genomics

Background:

  • Protein sequence alignment reveals conservation across species, highlighting critical functional regions.
  • Visualizing conserved domains alongside alignments enhances analysis of sequence conservation and functional motifs.

Purpose of the Study:

  • To develop a novel visualization approach for simultaneous analysis of protein sequence conservation and conserved domains.
  • To enable efficient identification of functionally important regions within protein sequences.

Main Methods:

  • MSAVis integrates multiple sequence alignment data with conserved domain information from the NCBI Conserved Domain Database (CDD).
  • The approach utilizes luminance and hue as visual cues for representing conservation strength and domain membership.
  • Software is implemented in Python, leveraging BioPython and OpenGL for visualization.

Main Results:

  • MSAVis provides a simultaneous visualization of conserved motifs and sequence alignment.
  • The tool facilitates both macro (sequence-wide) and micro (local neighborhood) views of conservation.
  • Enables at-a-glance summary of protein alignment conservation and comparisons among functional domains.

Conclusions:

  • MSAVis effectively uses preattentive and separable visual cues (luminance and hue) to represent conservation and domain information.
  • The visualization aids in understanding the relationship between conservation strength and domain membership.
  • The MSAVis software is publicly available for use in biological sequence analysis.