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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.
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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...

Protein Digestion

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Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.

Protein Networks

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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.
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Updated: Feb 10, 2026

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Using peptides to study protein-protein interactions.

Hadar Benyamini¹, Assaf Friedler

¹The Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem 91904, Israel.

Future Medicinal Chemistry

|March 24, 2011

Summary

This summary is machine-generated.

Studying protein-protein interactions (PPIs) is crucial for cell function and drug development. Using peptides simplifies PPI research, aiding in structural studies and the creation of drugs that modulate these interactions.

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Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Protein-protein interactions (PPIs) are fundamental to cellular processes.
Studying PPIs is vital for understanding diseases and developing therapeutics.
Expressing and purifying full-length proteins for PPI research presents significant challenges.

Purpose of the Study:

To highlight the utility of peptides in studying protein-protein interactions (PPIs).
To showcase experimental methods employed for peptide-based PPI studies.
To demonstrate the role of peptides in advancing PPI research and drug design.

Main Methods:

Peptide synthesis and characterization.
Biophysical techniques for analyzing peptide-PPIs (e.g., SPR, ITC).
Structural biology methods (e.g., X-ray crystallography, NMR) utilizing peptides.

Main Results:

Peptides offer a simplified approach to investigating PPIs compared to full-length proteins.
Peptide-based studies facilitate detailed structural and biophysical characterization of PPIs.
Peptides serve as valuable tools for identifying and designing modulators of PPIs.

Conclusions:

Peptides are effective tools for advancing the understanding of protein-protein interactions.
Peptide-based strategies significantly facilitate drug discovery efforts targeting PPIs.
The use of peptides streamlines PPI research, enabling more efficient structural and biophysical analyses.