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Protein Organization01:13

Protein Organization

Overview
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 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 and Protein Structure02:15

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...
Protein Folding01:25

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...

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Related Experiment Video

Updated: May 27, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Phase diagram of polypeptide chains.

Stefan Auer1

  • 1Centre for Molecular Nanoscience, School of Chemistry, University of Leeds, LS2 9JT Leeds, United Kingdom. s.auer@leeds.ac.uk

The Journal of Chemical Physics
|November 11, 2011
PubMed
Summary

This study reveals two stable peptide phases: solution and bulk fibrils. Metastable oligomeric phases exist, offering insights into polypeptide chain assembly in folded and unfolded states.

Area of Science:

  • Biophysics
  • Computational Biology
  • Materials Science

Background:

  • Understanding peptide self-assembly is crucial for various biological and material applications.
  • Natively folded (α-helical) and unfolded (β-sheet) conformations influence peptide phase behavior.
  • Characterizing peptide phase diagrams helps elucidate assembly mechanisms.

Purpose of the Study:

  • To determine the equilibrium phase diagram for natively folded α-helical and unfolded β-sheet forming peptides.
  • To identify all thermodynamically stable and metastable peptide phases.
  • To provide a framework for understanding peptide assembly.

Main Methods:

  • Utilized a coarse-grained protein model for simulations.
  • Calculated the equilibrium phase diagram of peptides.

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Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry

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Related Experiment Videos

Last Updated: May 27, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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

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Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry
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  • Analyzed the stability and metastability of different peptide phases.

    • Main Results:

    • Identified two thermodynamically stable peptide phases: peptide solution and bulk fibrillar phase.
    • Revealed the existence of multiple metastable peptide phases, including liquid-like oligomeric phases.
    • Established a hierarchy of metastability among the observed phases.
    • Demonstrated that oligomeric phases are metastable relative to fibrillar phases.

    Conclusions:

    • The phase diagram provides a comprehensive understanding of peptide assembly.
    • The findings are applicable to both natively folded and unfolded peptide conformations.
    • This work lays the groundwork for controlling peptide self-assembly processes.