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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

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Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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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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Updated: May 17, 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

Predicting turns in proteins with a unified model.

Qi Song¹, Tonghua Li, Peisheng Cong

¹Department of Chemistry, Tongji University, Shanghai, China.

|November 13, 2012

Summary

This study introduces TurnP, a unified model for predicting all protein turn types simultaneously. TurnP achieves high accuracy, outperforming existing methods for individual turn predictions.

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

Structural Biology
Bioinformatics
Computational Biology

Background:

Protein turns are essential structural motifs involved in protein folding and interactions.
Existing prediction methods focus on individual turn types, lacking a unified approach.
A simultaneous prediction model for all turn types is needed for comprehensive protein structure analysis.

Purpose of the Study:

To develop a novel, unified model for the simultaneous prediction of all protein turn types.
To improve the accuracy and efficiency of protein turn prediction.

Main Methods:

Developed TurnP, a unified model incorporating structural evolution information (secondary structure, shape strings) based on homology.
Utilized predicted secondary structures and shape strings generated by innovative technologies.
Generated sequence and structural evolution features through sequence and structure alignment.

Main Results:

TurnP achieved 88.8% accuracy and 71.8% sensitivity on a non-redundant dataset via five-fold cross-validation.
Performance exceeded state-of-the-art predictors for specific turn types.
Independent tests on EVA and CASP9 datasets demonstrated outstanding and practical performance.

Conclusions:

TurnP provides an accurate and unified approach for predicting all protein turns simultaneously.
The model's performance suggests significant advancements in protein structure prediction.
TurnP shows strong potential for practical applications in bioinformatics and structural biology.