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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
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...
Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...

You might also read

Related Articles

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

Sort by
Same author

A Comprehensive Dataset of Lipid Nanoparticle Compositions and Properties for Nucleic Acid Delivery.

Scientific data·2025
Same author

Announcement: Journal of Structural Biology: Paper of the year.

Journal of structural biology·2025
Same author

Thermodynamic Parameter Estimation for Modified Oligonucleotides Using Molecular Dynamics Simulations.

The journal of physical chemistry. B·2025
Same author

An accelerated molecular dynamics study for investigating protein pathways using the bond-boost hyperdynamics method.

Protein science : a publication of the Protein Society·2025
Same author

ELiAH: the atlas of E3 ligases in human tissues for targeted protein degradation with reduced off-target effect.

Database : the journal of biological databases and curation·2024
Same author

Protein-lipid acyl chain interactions: Depth-dependent changes of segmental mobility of phospholipid in contact with bacteriorhodopsin.

Biophysical chemistry·2024

Related Experiment Video

Updated: May 21, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

KOSMOS: a universal morph server for nucleic acids, proteins and their complexes.

Sangjae Seo1, Moon Ki Kim

  • 1Department of Nano Science and Technology and School of Mechanical Engineering, Sungkyunkwan University, 300, Cheoncheon-dong, Jangan-gu, Suwon 440-746, Korea.

Nucleic Acids Research
|June 7, 2012
PubMed
Summary

KOSMOS is a novel online server for analyzing macromolecular structural dynamics. It uniquely combines harmonic and anharmonic analyses, offering versatile coarse-graining and elastic network models for comprehensive molecular motion insights.

More Related Videos

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

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Related Experiment Videos

Last Updated: May 21, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

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

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Area of Science:

  • Structural Biology
  • Computational Biophysics
  • Bioinformatics

Background:

  • Understanding macromolecular structural dynamics is crucial for deciphering biological functions.
  • Existing tools often lack the versatility to analyze diverse molecular complexes and dynamics comprehensively.

Purpose of the Study:

  • To introduce KOSMOS, the first online morph server designed for comprehensive structural dynamics analysis of DNA/RNA, proteins, and their complexes.
  • To provide advanced tools for both harmonic and anharmonic analyses of macromolecular motion.

Main Methods:

  • Utilizes normal mode analysis (NMA) with elastic network models (ENM) for harmonic analysis, calculating vibrational modes and B-factors.
  • Employs elastic network interpolation (ENI) for anharmonic analysis to generate transition pathways between conformations.
  • Offers versatile coarse-graining methods and various ENM connection rules (distance-cutoff, number-cutoff, chemical-cutoff) for flexible model building.

Main Results:

  • KOSMOS enables detailed insights into potential biological functions through structural dynamics.
  • It generates plausible, sterically clash-free transition pathways between molecular conformations.
  • The server allows analysis with maximum degrees of freedom by integrating diverse ENM approaches.

Conclusions:

  • KOSMOS provides a powerful and versatile platform for studying macromolecular structural dynamics.
  • Its unique features in coarse-graining and ENM enhance the analysis of molecular motion and conformational changes.
  • The server facilitates a deeper understanding of the relationship between structure, dynamics, and biological function.