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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Fractal studies on the protein secondary structure elements
1Department of Biochemistry, University of Hyderabad, Hyderabad 500 046.
Indian Journal of Biochemistry & Biophysics
|August 9, 2013
Summary
Protein secondary structures exhibit distinct fractal dimensions, correlating with their abundance. Analysis reveals long-range correlations in protein sequences, potentially aiding prediction algorithms.
Area of Science:
- * Computational biology
- * Structural bioinformatics
- * Biophysics
Background:
- * Protein secondary structures are fundamental to protein folding and function.
- * Understanding the structural organization and sequence patterns is crucial for predicting protein properties.
- * Fractal analysis offers a novel approach to quantify the complexity of biological structures.
Purpose of the Study:
- * To calculate fractal dimensions for protein secondary structure elements.
- * To investigate the relationship between fractal dimensions and secondary structure abundance.
- * To explore sequence correlations using a Markov model.
Main Methods:
- * Calculation of fractal dimensions based on positional distributions of secondary structure elements.
- * Classification of secondary structure elements into distinct groups.
- * Application of a Markov model to analyze sequence transitions.
Main Results:
- * Seven secondary structure elements were grouped into two classes based on fractal dimensions.
- * A negative correlation was found between fractal dimension values and secondary structure abundances.
- * The Markov model indicated the presence of long-range correlations in protein sequences.
Conclusions:
- * Protein secondary structures display quantifiable complexity through fractal dimensions.
- * The identified correlations suggest underlying patterns in protein sequences.
- * These findings may enhance the development of protein prediction algorithms.
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