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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 Organization

Protein Organization

Protein and Protein Structure

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 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 locations, protein...

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Related Experiment Video

Updated: Jul 5, 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

PROTEUS2: a web server for comprehensive protein structure prediction and structure-based annotation.

Scott Montgomerie¹, Joseph A Cruz, Savita Shrivastava

¹Department of Computing Science and Department of Biological Sciences, University of Alberta and National Research Council, National Institute for Nanotechnology (NINT), Edmonton, AB, Canada T6G 2E8.

Nucleic Acids Research

|May 17, 2008

Summary

This summary is machine-generated.

PROTEUS2 is a powerful web server for protein structure prediction and annotation. It accurately identifies protein features like signal peptides and transmembrane helices, aiding biological research.

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Published on: November 3, 2011

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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

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

Published on: July 16, 2017

Area of Science:

Bioinformatics
Computational Biology
Structural Biology

Background:

Protein structure prediction is crucial for understanding protein function.
Accurate annotation of protein features aids in biological studies.
Existing tools often lack a comprehensive, integrated approach.

Purpose of the Study:

To introduce PROTEUS2, a web server for comprehensive protein structure prediction and annotation.
To integrate multiple prediction tasks into a single pipeline.
To provide accurate predictions for signal peptides, transmembrane regions, and protein structures.

Main Methods:

Utilizes progressive multi-sequence alignment and structure-based mapping.
Employs hidden Markov models and multi-component neural networks.
Leverages up-to-date databases for secondary structure assignments.

Main Results:

Achieves high predictive accuracy for signal peptides (Q2=94%) and transmembrane helices (Q2=87%).
Reports a Q3 score of 81.3% for secondary structure prediction.
Generates high-quality 3D homology models comparable to other leading tools (within 0.2 Å RMSD).

Conclusions:

PROTEUS2 offers a robust and integrated solution for protein structure prediction and annotation.
The server provides accurate predictions efficiently, with an average processing time of 3 minutes per sequence.
PROTEUS2 is accessible online with source code available for broader research use.