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

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...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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 Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Protein and Protein Structures02:15

Protein and Protein Structures

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 Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

You might also read

Related Articles

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

Sort by
Same author

Carbon distribution to toxic effect in toxin proteins.

Bioinformation·2012
Same author

Allotment of carbon is responsible for disorders in proteins.

Bioinformation·2011
Same author

CARBANA: Carbon analysis program forprotein sequences.

Bioinformation·2011
Same author

Role of large hydrophobic residues in proteins.

Bioinformation·2009
Same author

BIOFFORC: tool development for biological file format conversion.

Bioinformation·2009
Same author

Role of thymine in protein coding frames of mRNA sequences.

Bioinformation·2008
Same journal

Assessment of lower incisor position and symphysis dimensions among different skeletal patterns in the Chhattisgarh population.

Bioinformation·2026
Same journal

Low T3 syndrome and short-term outcomes in patients with acute decompensated heart failure: A retrospective observational study.

Bioinformation·2026
Same journal

Cardiovascular risk prevention awareness and practices in type 2 diabetes: Linking HbA1c and lipid levels.

Bioinformation·2026
Same journal

Assessment of periodontal condition using basic periodontal examination scores: A retrospective clinical study.

Bioinformation·2026
Same journal

Comparative evaluation of osseointegration among different surface modification techniques in dental implants.

Bioinformation·2026
Same journal

Micro-osteoperforations' impact on orthodontic tooth movement rate: Split mouth research.

Bioinformation·2026
See all related articles

Related Experiment Video

Updated: May 20, 2026

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
07:49

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

CARd: Carbon distribution analysis program for protein sequences.

Ekambaram Rajasekaran1

  • 1Department of Bioinformatics, School of Biotechnology and Health Sciences, Karunya University, Karunya Nagar, Coimbatore 641114.

Bioinformation
|July 26, 2012
PubMed
Summary
This summary is machine-generated.

Understanding protein structure and stability requires analyzing carbon distribution. A new program precisely identifies hydrophobic, hydrophilic, and disordered regions, aiding in mutation studies and protein stabilization.

Keywords:
carbon distributionhydropathyhydrophobic hydrophilicmutational studyprogramprotein disorder

More Related Videos

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

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Related Experiment Videos

Last Updated: May 20, 2026

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
07:49

Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

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

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein stability and structure are fundamentally governed by carbon distribution along the amino acid sequence.
  • The arrangement of amino acids, guided by messenger RNAs (mRNAs), dictates this carbon distribution.
  • An atomic-level understanding of these codes is crucial for deciphering protein function and disease mechanisms.

Purpose of the Study:

  • To develop a computational tool for analyzing carbon distribution at the atomic level within protein sequences.
  • To identify hydrophobic, hydrophilic, and disordered regions within proteins based on carbon distribution patterns.
  • To facilitate mutational studies and protein stabilization efforts through precise analysis.

Main Methods:

  • Development of a novel carbon distribution analysis program.
  • Utilizing atomic-level calculations to assess carbon distribution patterns.
  • Capturing and analyzing hydrophobic, hydrophilic, and disordered protein regions.

Main Results:

  • The developed program accurately identifies distinct protein regions based on carbon distribution.
  • Calculations demonstrate high precision and sensitivity, resolving single amino acid variations.
  • The program effectively delineates hydrophobic, hydrophilic, and disordered areas.

Conclusions:

  • The carbon distribution analysis program provides a precise method for studying protein structure and stability.
  • This tool aids in understanding the impact of mutations and can guide protein stabilization strategies.
  • Atomic-level insights into carbon distribution enhance the study of protein disorders and functional modifications.