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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.

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 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: May 11, 2026

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

mulPBA: an efficient multiple protein structure alignment method based on a structural alphabet.

Sylvain Léonard¹, Agnel Praveen Joseph, Narayanaswamy Srinivasan

¹a INSERM UMR-S 665, DSIMB , 6, rue Alexandre Cabanel, F-75739 , Paris , France .

Journal of Biomolecular Structure & Dynamics

|May 11, 2013

Summary

This summary is machine-generated.

Efficient protein structure comparison is crucial. The mulPBA web server uses a novel structural alphabet method for accurate multiple protein structure alignments, aiding functional and evolutionary analysis.

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Last Updated: May 11, 2026

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

An Integrated Approach for Microprotein Identification and Sequence Analysis

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

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

Area of Science:

Structural biology
Bioinformatics
Computational biology

Background:

The exponential growth of protein structure data necessitates advanced tools for comparative analysis.
Multiple structural alignments are fundamental for understanding protein function, evolution, and architecture.

Purpose of the Study:

To introduce mulPBA, a novel web server for efficient multiple protein structure alignment.
To provide a user-friendly platform for comparing protein structures based on their conformational properties.

Main Methods:

mulPBA employs a structural alphabet to represent protein backbone conformations as a 'sequence-like' string of dihedral angles.
It integrates sequence alignment algorithms for initial comparison, followed by iterative refinement of structural superposition.
The method is implemented in a web server for processing user-submitted protein structures.

Main Results:

The mulPBA approach achieves alignments superior to rigid-body methods and comparable to flexible structure comparison techniques.
The server provides sequence alignments, superposed 3D structures (PyMol/Jmol), quality measures, and a distance dendrogram.
Users can download superimposed structures in PDB format, with rapid result generation.

Conclusions:

mulPBA offers an effective and efficient method for multiple protein structure alignment.
The web server facilitates the analysis of protein structure, function, and evolution.
This tool is valuable for researchers in structural biology and bioinformatics.