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Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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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Related Experiment Video

Updated: Aug 16, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Polyelectrolyte Influence on Beta-Hairpin Peptide Stability: A Simulation Study.

Kevin Moses¹, Paul R Van Tassel¹

¹Dept. of Chemical and Environmental Engineering, Yale University, New Haven, Connecticut 06520-8286, United States.

The Journal of Physical Chemistry. B

|December 27, 2022

Summary

This summary is machine-generated.

Charged polymers impact protein stability. A lysine polymer stabilized one peptide while destabilizing another, revealing complex interactions crucial for designing new biomaterials.

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Last Updated: Aug 16, 2025

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Published on: November 21, 2013

Area of Science:

Biophysics
Materials Science
Computational Chemistry

Background:

Protein-polyelectrolyte assemblies are vital in pharmaceuticals and biotechnology.
Understanding polymer influence on protein structure and stability is key.

Purpose of the Study:

To investigate how charged polymers affect the thermal stability of model beta-hairpin peptides.
To elucidate the molecular mechanisms behind polymer-induced protein stabilization or destabilization.

Main Methods:

All-atom, replica exchange molecular dynamics simulations were performed.
Free energy profiles and statistical mechanical models (Ising-like) were utilized.

Main Results:

A cationic lysine polymer stabilized the Tryptophan Zipper 4 (TZ4) peptide but destabilized the Protein G B1 domain (GB1) peptide.
A cationic chitosan polymer showed minor stabilization for GB1 with no significant effect on TZ4.
Kinetic barriers separate folded and unfolded peptide states, influenced by polymer interactions.

Conclusions:

Polyelectrolyte interactions with proteins are complex, involving competition for hydrogen-bonding and hydrophobic interactions.
Findings inform the rational design of polyelectrolyte-based materials for biomedical applications.