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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 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 can...

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: Jun 15, 2026

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

Helix-sheet packing in proteins.

Chengcheng Hu¹, Patrice Koehl

¹Department of Computer Science, University of California, Davis, California 95616, USA.

|February 27, 2010

Summary

This summary is machine-generated.

This study analyzes protein alphabeta(2) motifs, detailing helix-sheet interactions and their geometry. Statistical potentials derived from this analysis improve protein structure prediction accuracy.

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Last Updated: Jun 15, 2026

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

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

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

Published on: November 21, 2013

Area of Science:

Protein structure and biophysics
Computational biology and bioinformatics

Background:

Protein three-dimensional structure relies on secondary structure element packing.
Helix-helix and sheet-sheet packing are well-understood, but helix-sheet interactions remain less characterized.

Purpose of the Study:

To analyze the conformation and geometry of alphabeta(2) motifs (helix in contact with two hydrogen-bonded beta-strands).
To derive statistical potentials for protein structure prediction based on observed helix-sheet interactions.

Main Methods:

Analysis of protein structures to identify and geometrically characterize alphabeta(2) motifs.
Quantification of azimuthal angle (theta), elevation angle (psi), and distance (D) in motifs.
Investigation of side-chain packing preferences at the helix-strand interface.

Main Results:

Helices show a tendency to align with beta-strands, preferring antiparallel orientation with parallel strands.
Hydrophobic interactions dominate the helix-strand interface, with specific amino acid preferences (aliphatic in strands, aromatic in helices).
Derived statistical potentials effectively distinguish native-like conformations from decoys.

Conclusions:

The geometry and amino acid propensities of alphabeta(2) motifs are crucial for understanding protein folding.
The developed statistical potentials offer a valuable tool for enhancing protein structure prediction accuracy.