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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Conserved Binding Sites01:49

Conserved Binding Sites

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 analyses the...
Protein Networks02:26

Protein Networks

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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Organization01:24

Protein Organization

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.
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jul 14, 2026

Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Bioinformatics approaches for disulfide connectivity prediction.

Chi-Hung Tsai1, Chen-Hsiung Chan, Bo-Juen Chen

  • 1Department of Chemical Engineering and Biotechnology and Graduate Institute of Biotechnology, National Taipei University of Technology, Taiwan.

Current Protein & Peptide Science
|June 23, 2007
PubMed
Summary

Predicting disulfide connectivity in proteins aids computational protein structure prediction by reducing conformational search space. This bioinformatics approach significantly improves accuracy for protein engineering and folding studies.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Area of Science:

  • Computational biology
  • Structural bioinformatics
  • Protein engineering

Background:

  • Protein structure prediction is crucial for understanding protein function and engineering novel proteins.
  • The vast conformational space of proteins presents a significant challenge in accurate structure prediction.
  • Disulfide bond information dramatically reduces search space and enhances prediction accuracy.

Purpose of the Study:

  • To review computational methods for predicting protein disulfide connectivity.
  • To analyze features and biological implications in disulfide bond prediction.
  • To discuss limitations and future prospects of disulfide bond prediction.

Main Methods:

  • Formulation of the disulfide connectivity prediction problem.
  • Review of computational techniques employed in the literature.
  • Analysis of features used for encoding protein information.

Main Results:

  • Disulfide connectivity prediction significantly refines protein structure prediction.
  • Feature selection and biological context are critical for prediction accuracy.
  • Identified limitations and challenges in current prediction methods.

Conclusions:

  • Accurate disulfide bond prediction is vital for advancing protein structure prediction and engineering.
  • Bioinformatics approaches offer powerful tools for predicting disulfide connectivity.
  • Future research should focus on overcoming limitations and expanding practical applications.