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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Ligand Binding Sites02:40

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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...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Globular and Fibrous Proteins02:21

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Protein Networks02:26

Protein Networks

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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.
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Protein Organization01:24

Protein Organization

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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.
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Related Experiment Video

Updated: Sep 19, 2025

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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BindUP-Alpha: A Webserver for Predicting DNA-and RNA-binding Proteins based on Experimental and Computational

Dina Alexandrovich1, Shani Kagan2, Yael Mandel-Gutfreund3

  • 1Technion-Israel Institute of Technology, Faculty of Biology, Emerson Building, Haifa, Israel.

Journal of Molecular Biology
|May 31, 2025
PubMed
Summary
This summary is machine-generated.

BindUP-Alpha predicts nucleic acid binding proteins using protein structure and surface electrostatics. This tool aids in characterizing protein function from both experimental and predicted structures.

Keywords:
DNA-binding proteinsRNA-binding proteinsfunction predictionmachine learning

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Area of Science:

  • Structural biology
  • Bioinformatics
  • Computational biology

Background:

  • Protein structure is crucial for function.
  • AI tools like AlphaFold generate many protein models.
  • Disordered regions in models challenge function prediction.

Purpose of the Study:

  • To present BindUP-Alpha, an upgraded webserver for predicting nucleic acid binding proteins.
  • To improve protein function characterization using predicted structures.

Main Methods:

  • Structure-based algorithm using electrostatic and physiochemical properties.
  • Support Vector Machine (SVM) learning approach.
  • Utilizes experimentally solved and predicted protein structures.

Main Results:

  • BindUP-Alpha accurately predicts DNA- and RNA-binding proteins.
  • Identifies potential nucleic acid binding interfaces on protein surfaces.
  • Successfully analyzes both experimental and AI-predicted protein models.

Conclusions:

  • BindUP-Alpha enhances the prediction of nucleic acid binding proteins.
  • Provides valuable insights into protein function from structural data.
  • Offers interactive visualizations and downloadable results via a webserver.