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Related Concept Videos

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...
Protein-protein Interfaces02:04

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 Organization01:24

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 Organization01:13

Protein Organization

Overview
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jun 6, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

A guide to UniProt for protein scientists.

Claire O'Donovan1, Rolf Apweiler

  • 1The European Bioinformatics Institute, Cambridge, UK.

Methods in Molecular Biology (Clifton, N.J.)
|November 18, 2010
PubMed
Summary

The Universal Protein Resource (UniProt) offers high-quality, annotated protein databases crucial for proteomics research. It provides stable identifiers and archival services for protein identification and characterization.

Area of Science:

  • Proteomics and Bioinformatics

Background:

  • The proteomics community requires high-quality, annotated, non-redundant protein sequence databases.
  • Stable identifiers and archival services are essential for protein identification and characterization.

Purpose of the Study:

  • To illustrate the optimal utilization of the Universal Protein Resource (UniProt) for proteomics applications.
  • To highlight the exploitation of knowledge within UniProt databases, its services, and complete proteomes.

Main Methods:

  • Focus on leveraging the comprehensive data within UniProt.
  • Utilizing UniProt's provided services for data access and analysis.
  • Exploring the availability of complete proteomes for research.

Main Results:

  • UniProt serves as a vital resource for proteomics.

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Last Updated: Jun 6, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
07:49

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

Published on: August 16, 2017

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

  • Knowledge captured in UniProt facilitates protein identification and characterization.
  • Complete proteomes enhance the scope of proteomics studies.

    • Conclusions:

    • UniProt is an indispensable tool for the proteomics community.
    • Effective utilization of UniProt enhances research capabilities in protein science.
    • UniProt's comprehensive resources support advanced proteomics investigations.