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 Organization01:24

Protein Organization

9.0K
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....
9.0K
Protein Families02:47

Protein Families

16.6K
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...
16.6K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.0K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.6K
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
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K

You might also read

Related Articles

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

Sort by
Same author

The effectiveness of tissue-perfusion-guided resuscitation in shock: A systematic review and meta-analysis.

Annals of intensive care·2026
Same author

A Single Amino Acid Substitution Reprograms ROS Selectivity and Catalytic Function in DyP Peroxidases.

Inorganic chemistry·2026
Same author

Analytical Robustness and Competing Interpretations in Violent Video Game Research: A Response to Teng and Bushman's (2026) Reanalysis of Lacko et al. (2024).

Aggressive behavior·2026
Same author

Ecological Context Shapes Resistance Selection Under Antibiotic Pollution.

Environmental microbiology·2026
Same author

Beyond the overt response: Reaction time modeling in self-report surveys across administration modes and item formats.

Behavior research methods·2026
Same author

EnzymeMiner 2.0: advancing automated enzyme discovery with expansive sequence mining and smart property analysis.

Nucleic acids research·2026

Related Experiment Video

Updated: Jan 6, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.5K

FireProtDB 2.0: large-scale manually curated database of the protein stability data.

Milos Musil1,2,3, Simeon Borko1,3, Joan Planas-Iglesias1,3

  • 1Loschmidt Laboratories, Department of Experimental Biology and RECETOX, Masaryk University, 625 00, Brno, Czech Republic.

Nucleic Acids Research
|November 20, 2025
PubMed
Summary

FireProtDB 2.0 enhances protein stability research by providing a vastly expanded database of experimental data. This resource supports computational methods for developing more robust proteins for various applications.

More Related Videos

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

29.1K
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

16.0K

Related Experiment Videos

Last Updated: Jan 6, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.5K
How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

29.1K
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

16.0K

Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Biotechnology

Background:

  • Thermostable proteins are vital for biomedical and biotechnological applications.
  • Improving protein stability through lab experiments is costly and time-consuming.
  • Computational methods offer a scalable alternative but require high-quality data.

Purpose of the Study:

  • To present FireProtDB 2.0, an updated large-scale database for protein stability data.
  • To expand the database's capacity for diverse mutation types and data formats.
  • To improve data accessibility and usability in accordance with FAIR principles.

Main Methods:

  • Aggregation of protein stability data from multiple sources.
  • Implementation of a new data storage and maintenance scheme.
  • Inclusion of absolute and relative data types for various protein constructs and mutations.

Main Results:

  • The database size increased from 16,000 to nearly 5,500,000 experiments.
  • Support for complex mutations (insertions, deletions, multiple-point) was added.
  • The abstract scheme is fully expandable for new measurements and annotations.

Conclusions:

  • FireProtDB 2.0 significantly enhances the availability of high-quality protein stability data.
  • The expanded database supports more reliable computational prediction of protein stability.
  • The updated structure and FAIR compliance facilitate data integration and reuse.