A tetrapeptide-based method for polyproline II-type secondary structure prediction
Related Experiment Video
Updated: Aug 15, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Peter K Vlasov1, Anna V Vlasova, Vladimir G Tumanyan
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. vlasov@imb.ac.ru
Abstract:
We describe a new method for polyproline II-type (PPII) secondary structure prediction based on tetrapeptide conformation properties using data obtained from all globular proteins in the Protein Data Bank (PDB). This is the first method for PPII prediction with a relatively high level of accuracy (approximately 60%). Our method uses only frequencies of different conformations among oligopeptides without any additional parameters. We also attempted to predict alpha-helices and beta-strands using the same approach. We find that the application of our method reveals interrelation between sequence and structure even for very short oligopeptides (tetrapeptides).
More Related Videos
Related Concept Videos
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.
Protein Folding
Protein Folding
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 and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...

