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Related Concept Videos

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 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.
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Published on: July 25, 2013

A homology/ab initio hybrid algorithm for sampling near-native protein conformations.

Priyanka Dhingra1, Bhyravabhotla Jayaram

  • 1Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India.

Journal of Computational Chemistry
|June 4, 2013
PubMed
Summary

A new hybrid algorithm, Bhageerath-H Strgen, improves protein tertiary structure prediction by enhancing conformational sampling. It efficiently generates near-native protein structures using homology and ab initio methods.

Keywords:
ab initio modelingfold recognitionhomology modelingloop modelingprotein foldingprotein tertiary structure prediction

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Published on: July 14, 2015

Area of Science:

  • Computational Biology
  • Structural Bioinformatics
  • Protein Structure Prediction

Background:

  • Protein tertiary structure prediction is crucial for understanding protein function.
  • Current conformational sampling algorithms face challenges in efficiently searching protein fold space.
  • Integrating homology, fold recognition, and ab initio methods can improve prediction accuracy.

Purpose of the Study:

  • To develop Bhageerath-H Strgen, a hybrid algorithm for enhanced protein conformational sampling.
  • To improve the generation of near-native protein conformations.
  • To provide a web-accessible tool for protein decoy generation.

Main Methods:

  • Developed Bhageerath-H Strgen, a homology/ab initio hybrid algorithm.
  • Tested the algorithm on the CASP9 dataset comprising 116 protein targets.
  • Evaluated the efficiency and performance against other decoy generation methods.

Main Results:

  • Bhageerath-H Strgen generated structures with a TM-score ≥ 0.5 in 93% of tested cases.
  • The algorithm demonstrated efficient performance compared to existing decoy generation methods.
  • A web tool for Bhageerath-H Strgen is now freely accessible.

Conclusions:

  • Bhageerath-H Strgen effectively enhances protein conformational sampling.
  • The hybrid approach offers an efficient strategy for generating near-native protein structures.
  • The web tool facilitates broader access to advanced protein decoy generation capabilities.