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Updated: Apr 17, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Template-based prediction of protein function
Donald Petrey1, T Scott Chen1, Lei Deng1
1Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Department of Systems Biology, Center for Computational Biology and Bioinformatics, 1130 St. Nicholas Avenue, Room 815, New York, NY 10032, United States.
Structure-based protein function annotation uses known protein structures to predict the function of new proteins. Recent advances enable proteome-wide analysis, expanding beyond traditional sequence comparison methods.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Protein function annotation is crucial for understanding biological systems.
- Template-based methods infer function from known structures and functions.
- Traditional methods rely heavily on sequence similarity.
Purpose of the Study:
- To review recent advances in structure-based protein function annotation.
- To highlight template-based methods and template identification strategies.
- To discuss the expanding applicability of structural information in function prediction.
Main Methods:
- Focus on template-based approaches for protein function annotation.
- Discuss template identification via sequence analysis.
- Introduce structure-based similarity methods for template identification.
- Leverage homology modeling and structural information.
Main Results:
- Structure-based methods now complement and expand upon sequence-based approaches.
- New methods identify functional relationships missed by sequence analysis.
- Proteome-wide application of template-based methods is increasingly feasible.
- Structural information significantly broadens function annotation capabilities.
Conclusions:
- Structure-based protein function annotation is rapidly advancing.
- Template-based methods, especially those using structural similarity, are powerful tools.
- These advancements enhance our ability to annotate protein functions across entire proteomes.
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