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Protein Organization

Protein Organization

Protein Folding

Protein Folding

Protein Organization

Protein Organization

Protein Folding

Protein Folding

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 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...

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Related Experiment Video

Updated: Jul 7, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Context-dependent secondary structure formation of a designed protein sequence

D L Minor¹, P S Kim

¹Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.

|April 25, 1996

Summary

Non-local interactions, not just local preferences, can dictate protein secondary structure. A designed

Area of Science:

Protein structure and folding dynamics.
Biophysics and molecular biology.

Background:

Protein secondary structures (alpha-helices and beta-sheets) are key to protein folding.
Amino acid propensities for secondary structures are influenced by local and non-local factors.

Purpose of the Study:

To investigate the influence of non-local factors on protein secondary structure formation.
To design and test a peptide sequence whose secondary structure is context-dependent.

Main Methods:

Designed an 11-amino-acid 'chameleon' sequence.
Inserted the sequence into different positions within the IgG-binding domain of protein G (GB1).
Assessed protein folding and structure using biophysical criteria.

Main Results:

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The 'chameleon' sequence adopted an alpha-helix in one position and a beta-sheet in another.
Both resulting proteins (chameleon-alpha and chameleon-beta) exhibited native-like structures.
Demonstrated that non-local interactions can determine secondary structure for significant peptide lengths.

Conclusions:

Non-local interactions play a crucial role in determining protein secondary structure.
Tertiary interactions are likely dominant factors in protein folding and overall structure.