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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

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-Protein Interfaces

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Related Experiment Video

Updated: Jun 27, 2026

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

The Protein Model Portal.

Konstantin Arnold¹, Florian Kiefer, Jürgen Kopp

¹Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056, Basel, Switzerland.

Journal of Structural and Functional Genomics

|November 28, 2008

Summary

This summary is machine-generated.

The Protein Model Portal (PMP) integrates millions of protein structure models from diverse sources. This resource simplifies access to comparative modeling data, aiding protein structure exploration.

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Published on: July 25, 2013

Related Experiment Videos

Last Updated: Jun 27, 2026

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

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

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
Computational biology
Bioinformatics

Background:

High-throughput structural genomics yields many protein structures, but known sequences far exceed solved structures.
Homology modeling uses known structures to predict structures of related proteins, complementing experimental data.
Accessing diverse, pre-computed protein models across different databases and formats has been a significant challenge.

Purpose of the Study:

To create a unified portal for accessing a vast collection of protein structure models.
To overcome challenges in data accessibility due to heterogeneous formats and incompatible accession codes.
To facilitate the exploration of protein structure space by integrating experimental and modeled structures.

Main Methods:

Development of the Protein Model Portal (PMP) as a single access point.
Integration of pre-computed models from multiple partner resources (e.g., CSMP, ModBase, SWISS-MODEL Repository).
Provision of a unified interface for querying models and linking to related services (template selection, alignment, quality assessment).

Main Results:

The PMP provides access to 7.6 million pre-computed protein model structures.
A single interface allows simultaneous querying of models from various distributed resources.
Links to interactive services enhance the utility of the model data.

Conclusions:

The Protein Model Portal significantly improves access to and utilization of protein structure models.
PMP aids researchers in exploring protein structure-function relationships by consolidating modeling data.
This resource complements experimental structure determination efforts in structural genomics.