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

Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

4.6K
Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved...
4.6K
Conserved Binding Sites01:49

Conserved Binding Sites

1.9K
1.9K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.0K
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...
14.0K
Conformations of Ethane and Propane02:18

Conformations of Ethane and Propane

16.8K
In an organic molecule, free rotation about the carbon-carbon single bond results in energetically different conformers of the molecule. Due to this rotation, called the internal rotation, ethane has two major conformations — staggered and eclipsed.
Staggered conformation is a low energy and more stable conformation with the C-H bonds on the front carbon placed at 60°dihedral angles relative to the C-H bonds on the back carbon, leading to a reduced torsional strain. In staggered...
16.8K
Conformations of Cyclohexane02:11

Conformations of Cyclohexane

15.2K
Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
15.2K

You might also read

Related Articles

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

Sort by
Same author

Insights from aquaporin structures into drug-resistant sleeping sickness.

eLife·2026
Same author

The Inaugural Flatiron Institute Cryo-EM Conformational Heterogeneity Challenge.

bioRxiv : the preprint server for biology·2025
Same author

How many (distinguishable) classes can we identify in single-particle analysis?

Acta crystallographica. Section D, Structural biology·2025
Same author

ISG15 as a Potent Immune Adjuvant in MVA-Based Vaccines Against Zika Virus and SARS-CoV-2.

Vaccines·2025
Same author

Structural analysis of HER2-trastuzumab complex reveals receptor conformational adaptation.

Science advances·2025
Same author

Real-space heterogeneous reconstruction, refinement, and disentanglement of CryoEM conformational states with HetSIREN.

Nature communications·2025
Same journal

Spatio-DARLIN enables robust and efficient in situ lineage tracing in mice at single-cell resolution.

Nature methods·2026
Same journal

EasyGrid: a versatile platform for automated cryo-EM sample preparation and quality control.

Nature methods·2026
Same journal

Cloud-based microscope enables live neuroimaging for 24 h and beyond with worldwide access.

Nature methods·2026
Same journal

Deep molecular profiling in three dimensions.

Nature methods·2026
Same journal

3D pathology-guided microdissection.

Nature methods·2026
Same journal

Challenges and recommendations in establishing national human diversity genomic projects.

Nature methods·2026
See all related articles

Related Experiment Video

Updated: Jan 16, 2026

Spatial Separation of Molecular Conformers and Clusters
10:37

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

11.7K

Merging conformational landscapes in a single consensus space with FlexConsensus algorithm.

David Herreros1, Carlos Perez Mata2, Carlos Oscar Sanchez Sorzano3

  • 1Centro Nacional de Biotecnologia-CSIC, Madrid, Spain. dherreros@cnb.csic.es.

Nature Methods
|September 25, 2025
PubMed
Summary
This summary is machine-generated.

FlexConsenus integrates multiple structural heterogeneity algorithms in cryo-EM, creating a reliable consensus space. This approach enhances the accuracy and interpretability of protein conformational landscapes from experimental data.

More Related Videos

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

7.7K
Cryo-EM and Single-Particle Analysis with Scipion
09:06

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

4.3K

Related Experiment Videos

Last Updated: Jan 16, 2026

Spatial Separation of Molecular Conformers and Clusters
10:37

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

11.7K
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

7.7K
Cryo-EM and Single-Particle Analysis with Scipion
09:06

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

4.3K

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Cryo-electron microscopy (cryo-EM) structural heterogeneity analysis is advancing, enabling more accurate conformational landscape estimations.
  • New methods aim to improve understanding of protein dynamics, but direct comparison of heterogeneity algorithms is lacking.
  • Assessing algorithm reliability is crucial for validating conformational landscape interpretations.

Purpose of the Study:

  • To develop a method for comparing and integrating different structural heterogeneity algorithms in cryo-EM.
  • To create a shared consensus space for multiple conformational landscapes.
  • To enhance the reliability and interpretability of cryo-EM derived structural variability.

Main Methods:

  • Introduction of FlexConsenus, a multi-autoencoder neural network.
  • Learning commonalities and differences among various conformational landscapes.
  • Mapping multiple landscapes into a unified consensus space.

Main Results:

  • FlexConsenus successfully integrates diverse conformational landscapes into a reliable consensus space.
  • The consensus space allows for the measurement of reproducibility in heterogeneity estimations.
  • Enables focused analysis on stable structural variability or method-specific particle subsets.

Conclusions:

  • FlexConsenus provides a robust framework for comparing and consolidating structural heterogeneity analyses in cryo-EM.
  • Facilitates more reliable interpretation of protein conformational dynamics.
  • Improves the overall accuracy and trustworthiness of cryo-EM structural studies.