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

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.0K
10.0K
Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
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...
5.2K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.6K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.6K
Nuclear Binding Energy02:13

Nuclear Binding Energy

14.8K
The difference between the calculated and experimentally measured masses is known as the mass defect of the atom. In the case of helium-4, the mass defect indicates a “loss” in mass of 4.0331 amu – 4.0026 amu = 0.0305 amu. The loss in mass accompanying the formation of an atom from protons, neutrons, and electrons is due to the conversion of that mass into energy that is evolved as the atom forms. The nuclear binding energy is the energy produced when the atoms’ nucleons are bound...
14.8K
Ligand Binding Sites02:40

Ligand Binding Sites

15.1K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.1K

You might also read

Related Articles

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

Sort by
Same author

A BODIPY-based turn-on fluorescent probe for the selective detection of hydrogen sulfide in solution and in cells.

Talanta·2015
Same author

Analysis of sagittal balance using spinopelvic parameters in ankylosing spondylitis patients treated with vertebral column decancellation surgery.

Acta orthopaedica Belgica·2015
Same author

Using a 3D Culture System to Differentiate Visceral Adipocytes In Vitro.

Endocrinology·2015
Same author

Noncontact Monitoring of Blood Oxygen Saturation Using Camera and Dual-Wavelength Imaging System.

IEEE transactions on bio-medical engineering·2015
Same author

Digital human modeling and its applications: Review and future prospects.

Journal of X-ray science and technology·2015
Same author

Capture-based high-coverage NGS: a powerful tool to uncover a wide spectrum of mutation types.

Genetics in medicine : official journal of the American College of Medical Genetics·2015
Same journal

Correction to 'New origin firing is inhibited by APC/CCdh1 activation in S-phase after severe replication stress'.

Nucleic acids research·2026
Same journal

VeloRM: disentangling pre- and post-splicing RNA modification dynamics at single-cell resolution.

Nucleic acids research·2026
Same journal

Accessibility of telomeric overhangs to stabilizing small-molecule ligands.

Nucleic acids research·2026
Same journal

Multivalent interactions mediate SNAIL transcription factor stimulation of the nucleosome deacetylase activity of the CoREST complex.

Nucleic acids research·2026
Same journal

Genome-wide mapping of DNA G-quadruplexes in Trypanosoma brucei chromatin reveals enrichment in coding regions and transcription start sites.

Nucleic acids research·2026
Same journal

Correction to 'The Gene Ontology knowledgebase in 2026'.

Nucleic acids research·2026
See all related articles

Related Experiment Video

Updated: Jan 31, 2026

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
12:24

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

54.2K

beRBP: binding estimation for human RNA-binding proteins.

Hui Yu1, Jing Wang1,2, Quanhu Sheng1,2

  • 1Center for Quantitative Sciences, Vanderbilt University Medical Center, Nashville, TN 37232, USA.

Nucleic Acids Research
|December 28, 2018
PubMed
Summary
This summary is machine-generated.

We developed beRBP, a dual computational approach to predict RNA-binding protein (RBP) interactions. It offers accurate predictions for both well-studied and novel RBPs, enhancing our understanding of RBP functions.

More Related Videos

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.1K
An Assay for Quantifying Protein-RNA Binding in Bacteria
07:02

An Assay for Quantifying Protein-RNA Binding in Bacteria

Published on: June 12, 2019

7.0K

Related Experiment Videos

Last Updated: Jan 31, 2026

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
12:24

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

54.2K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.1K
An Assay for Quantifying Protein-RNA Binding in Bacteria
07:02

An Assay for Quantifying Protein-RNA Binding in Bacteria

Published on: June 12, 2019

7.0K

Area of Science:

  • Computational biology
  • Molecular biology
  • Bioinformatics

Background:

  • Understanding RNA-binding protein (RBP) interactions is crucial for elucidating their functional mechanisms.
  • Current computational methods for predicting RBP-RNA interactions often involve machine learning, facing a trade-off between prediction accuracy (RBP-specific models) and broad applicability (pooled RBP-RNA interaction models).
  • RBP-specific models require substantial known targets, limiting their use, while pooled models obscure crucial interaction features, reducing accuracy.

Purpose of the Study:

  • To present beRBP, a novel dual computational approach for predicting human RBP-RNA interactions.
  • To provide a tool that can accurately predict interactions for both RBPs with abundant known targets and those with limited or no known targets.
  • To improve the scope and accuracy of computational RBP binding estimation.

Main Methods:

  • beRBP utilizes a dual approach based on Random Forests.
  • It builds RBP-specific models for proteins with sufficient known targets.
  • It develops a general model for RBPs with limited or null known targets, using PWM of a RBP and an RNA sequence.

Main Results:

  • Both the specific and general models of beRBP demonstrated strong performance compared to existing methods on benchmark datasets.
  • The general model of beRBP outperformed existing methods on most novel RBPs.
  • beRBP offers a composite solution that integrates RBP-specific and general prediction strategies.

Conclusions:

  • beRBP is a promising computational tool for estimating human RBP binding.
  • The dual approach of beRBP provides good prediction accuracy and a broad application scope.
  • This tool facilitates a deeper understanding of RBP functional mechanisms through accurate binding site prediction.