Related Experiment Video
Updated: Aug 1, 2026

16:41
A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Repeat protein architectures predicted by a continuum representation of fold space
Andrew C Hausrath1, Alain Goriely
1Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, 85721, USA. hausrath@email.arizona.edu
Protein Science : a Publication of the Protein Society
|March 9, 2006
Summary
Researchers explored protein fold possibilities using a novel mapping method for helical repeats. This systematic approach identified both existing and new protein folds, advancing our understanding of protein architecture.
Area of Science:
- * Structural biology
- * Bioinformatics
- * Computational chemistry
Background:
- * The complete set of possible protein folds remains an open question in structural biology.
- * Understanding the diversity of protein architectures is crucial for predicting protein function and designing novel proteins.
Purpose of the Study:
- * To develop a systematic method for exploring the protein fold space of helical repeats.
- * To determine if all possible helical repeat protein folds have been realized in nature.
Main Methods:
- * Developed a mapping between repetitive curves and a parameter space defining these curves.
- * Explored the parameter space for the helical repeat protein architecture.
- * Analyzed a planar subspace of the helical repeat parameter space.
Main Results:
- * Identified specific points within the parameter space corresponding to naturally occurring helical repeat protein folds.
- * Discovered points in the parameter space representing potential helical repeat folds not yet observed in nature.
- * Demonstrated a method for systematically exploring fold space within a specific protein architecture.
Conclusions:
- * The study provides a framework for systematically exploring the potential protein fold space.
- * Findings suggest that nature may not have utilized all possible helical repeat protein folds.
- * The identified novel folds represent targets for future experimental validation and protein design.
Related Concept Videos
Protein Folding
Overview
Protein Folding
Overview
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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

