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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

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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...

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Related Experiment Video

Updated: Jul 17, 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

On the relationship between sequence and structure similarities in proteomics.

Evgeny Krissinel¹

¹European Bioinformatics Institute, Genome Campus, Hinxton, Cambridge CB10 1SD, UK. keb@ebi.ac.ukkeb

Bioinformatics (Oxford, England)

|January 24, 2007

Summary

Protein structure is tolerant to sequence changes that preserve hydropathic profiles, explaining sequence similarity thresholds in proteomics. This finding advances our understanding of protein sequence-structure relationships.

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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:

Proteomics
Structural Biology
Bioinformatics

Background:

Comparative studies in proteomics often assume protein structure and function link to sequence motifs.
The precise relationship between protein sequence and structure remains complex and not fully understood.

Purpose of the Study:

To investigate the relationship between protein sequence and structure.
To explain the observed sequence similarity thresholds in structural resemblance studies.

Main Methods:

Statistical analysis of multiple and pairwise structural alignments.
Analysis performed on protein structures within the Structural Classification of Proteins (SCOP) folds.

Main Results:

Conservation of exact residue identity is not common across related protein structures.
A model explaining sequence-structure relationships based on hydropathic profile conservation is proposed.
This model accounts for the sequence similarity threshold below which structural resemblance is not statistically expected.

Conclusions:

Protein structure tolerance to residue substitutions preserving hydropathic profiles is a key factor in sequence-structure relationships.
The proposed model provides a framework for understanding sequence similarity thresholds in proteomics.