Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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 Folding01:22

Protein Folding

Overview
Conservation of Protein Domains Over Different Proteins02:26

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...
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.
Protein Organization01:13

Protein Organization

Overview

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Interplay of self, epiphany, and positive actions in shaping individual careers.

Physical review. E·2023
Same author

Stock market efficiency: An intraday case of study about the G-20 group.

Heliyon·2022
Same author

A data-driven model for COVID-19 pandemic - Evolution of the attack rate and prognosis for Brazil.

Chaos, solitons, and fractals·2021
Same author

Non-Arrhenius behavior and fragile-to-strong transition of glass-forming liquids.

Physical review. E·2020
Same author

Characterization of the non-Arrhenius behavior of supercooled liquids by modeling nonadditive stochastic systems.

Physical review. E·2019
Same author

Statistical test for <math></math> : Methods and data.

Data in brief·2018

Related Experiment Video

Updated: Jun 18, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Self-similarity and protein compactness.

M A Moret1, M C Santana, G F Zebende

  • 1Programa de Modelagem Computacional, SENAI CIMATEC, Salvador, BA, Brazil. mamoret@gmail.com

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|November 13, 2009
PubMed
Summary
This summary is machine-generated.

Protein folding is driven by the hydrophobic effect, leading to a compact structure. Fractal analysis reveals that protein solvent-accessible surface area exhibits self-similarity, similar to crumpled wires.

More Related Videos

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

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

Related Experiment Videos

Last Updated: Jun 18, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

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

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • The hydrophobic effect is a primary driver of protein folding and the formation of a compact, shielded hydrophobic core.
  • The solvent-accessible surface area (SASA) of a protein is a key characteristic influenced by its folded state.

Purpose of the Study:

  • To analyze the self-similarity and scaling properties of protein SASA.
  • To investigate the relationship between SASA, protein size (number of amino acids), and compactness (radius of gyration).
  • To determine if fractal analysis can effectively describe protein compactness.

Main Methods:

  • Analysis of SASA for 1825 non-homologous protein chains from the Brookhaven Protein Data Bank.
  • Comparison of SASA as a function of amino acid count and SASA as a function of gyration radius.
  • Calculation of scaling exponents to quantify self-similarity.

Main Results:

  • Protein SASA exhibits intrinsic self-similarity.
  • The scaling exponent derived from SASA analysis closely matches exponents observed for volume-radius of gyration and mass-size relationships.
  • Fractal analysis provides a quantitative measure of protein compactness.

Conclusions:

  • Protein compactness can be effectively described using fractal analysis.
  • The folding of proteins results in a SASA that behaves like an object packed between random spheres at the percolation threshold or like crumpled wires.
  • This study highlights the utility of fractal geometry in understanding protein structure and folding.