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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.
A protein's shape is critical to its function. For example, an enzyme...

Protein Folding

Protein Folding

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 Folding

Protein Folding

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....

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Related Experiment Video

Updated: Apr 11, 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

Secondary structure and rigidity in model proteins.

Stefania Perticaroli¹, Jonathan D Nickels, Georg Ehlers

¹aChemical and Materials Sciences Division at Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.

|June 2, 2015

Summary

This summary is machine-generated.

The beta-sheet motif is stiffer than the alpha-helix in proteins, impacting their rigidity and dynamics. Protein secondary structure influences temperature and hydration effects on protein mechanics.

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Last Updated: Apr 11, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction

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Published on: November 3, 2011

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

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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Published on: July 16, 2017

Area of Science:

Biophysics
Structural Biology
Protein Science

Background:

Protein secondary structures, including alpha-helices and beta-sheets, are fundamental to protein folding and function.
Understanding the nanomechanical properties of these structures is crucial for comprehending protein dynamics and stability.

Purpose of the Study:

To investigate the relationship between protein secondary structure and nanomechanical properties.
To compare the rigidity and dynamics of alpha-helices and beta-motifs in model proteins.

Main Methods:

Analysis of nanomechanical properties of selected model proteins representing distinct secondary structures (alpha-helices, beta-barrels, alpha + beta structures).
Experimental evaluation in both dry and hydrated states.

Main Results:

The beta-sheet motif exhibits greater stiffness compared to the alpha-helix in model proteins, irrespective of hydration.
Secondary structure correlates with temperature- and hydration-induced changes in protein dynamics and rigidity.
A link between alpha-helix length and the boson peak (low-frequency vibrational mode) was observed.

Conclusions:

Protein secondary structure plays an intimate role in determining protein dynamics and rigidity.
The findings provide insights into how structural motifs influence macroscopic mechanical properties of proteins.