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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.
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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.
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Related Experiment Video

Updated: Oct 13, 2025

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

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DeepREx-WS: A web server for characterising protein-solvent interaction starting from sequence.

Matteo Manfredi1, Castrense Savojardo1, Pier Luigi Martelli1

  • 1Biocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy.

Computational and Structural Biotechnology Journal
|November 12, 2021
PubMed
Summary

This study introduces DeepREx-WS, a web server integrating protein residue exposure, conservation, flexibility, and disorder. It aids in identifying key regions for protein surface engineering and stability modification.

Keywords:
Deep LearningProtein disorderProtein flexibilityResidue solvent accessibilitySurface engineering

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Protein Engineering

Background:

  • Protein structure and function are influenced by residue exposure and flexibility.
  • Understanding protein-solvent interactions is crucial for surface engineering, especially when structural data is limited.

Purpose of the Study:

  • To develop a web server (DeepREx-WS) that integrates multiple features for analyzing protein residue properties.
  • To provide a tool for identifying critical regions in protein sequences for stability modification and surface engineering.

Main Methods:

  • Development of DeepREx, a deep learning tool for classifying residues as buried or exposed.
  • Integration of DeepREx predictions with residue conservation, hydrophobicity, flexibility, secondary structure, and disorder data.
  • Benchmarking DeepREx on a diverse dataset from the Protein Data Bank.

Main Results:

  • DeepREx achieves state-of-the-art performance in residue exposure prediction.
  • DeepREx-WS offers a comprehensive platform for analyzing protein sequence features.
  • The server facilitates the identification of residues for targeted protein modification.

Conclusions:

  • DeepREx-WS enhances the understanding of protein integrity by combining diverse sequence and structural features.
  • The web server is a valuable resource for protein surface engineering and biotechnological applications.
  • Integrating residue exposure with other properties aids in rational protein design.