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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 form...

Protein Organization

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 Organization

Protein Organization

Protein Organization

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 Folding

Protein Folding

Protein Folding

Protein Folding

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Related Experiment Video

Updated: May 22, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

DSP: a protein shape string and its profile prediction server.

Jiangming Sun¹, Shengnan Tang, Wenwei Xiong

¹Department of Chemistry, Tongji University, 1239 Siping Road, Shanghai 200092, China.

Nucleic Acids Research

|May 4, 2012

Summary

We developed an accurate protein shape string predictor using novel sequence alignment and profile methods. This tool aids in detailed protein structure analysis and evolution studies.

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A Protocol for Computer-Based Protein Structure and Function Prediction

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

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

Published on: July 25, 2013

Area of Science:

Structural Biology
Bioinformatics

Background:

Shape string is a crucial protein structure representation, offering more detail than secondary structures, especially in random coil regions.
Existing services for systematic protein shape string analysis are limited.

Purpose of the Study:

To develop an accurate predictor for protein shape strings.
To provide a systematic analysis service for protein shape strings.

Main Methods:

Developed a knowledge-driven sequence alignment technique.
Implemented a sequence shape string profile method.
Created the DSP (Database for Shape string Prediction) server.

Main Results:

The predictor demonstrated high accuracy on blind test data.
The DSP server provides predicted shape strings and sequence shape string profiles.
Users can compare protein structures and visualize evolution in shape string space.

Conclusions:

The developed method enables accurate protein shape string prediction.
The DSP server offers valuable tools for structural and evolutionary analysis of proteins.