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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:13

Protein Organization

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Protein Organization01:24

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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Related Experiment Video

Updated: May 9, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Fractal studies on the protein secondary structure elements.

Y Surya Pavan1, C K Mitra

  • 1Department of Biochemistry, University of Hyderabad, Hyderabad 500 046.

Indian Journal of Biochemistry & Biophysics
|August 9, 2013
PubMed
Summary
This summary is machine-generated.

Protein secondary structures exhibit distinct fractal dimensions, correlating with their abundance. Analysis reveals long-range correlations in protein sequences, potentially aiding prediction algorithms.

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Related Experiment Videos

Last Updated: May 9, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

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.