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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 Networks02:26

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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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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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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Ribosome Profiling02:24

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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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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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    Area of Science:

    • Computational biology
    • Bioinformatics
    • Genomics

    Background:

    • Protein-DNA interactions are vital for biological processes like transcription and replication.
    • Predicting DNA binding sites in proteins is established, but predicting protein binding sites in DNA is less explored.

    Purpose of the Study:

    • To identify features for predicting protein binding sites within DNA sequences.
    • To develop computational models for predicting protein binding nucleotides in DNA.

    Main Methods:

    • Analysis of protein-DNA complex structures.
    • Development of two support vector machine (SVM) models using DNA sequences alone and combined DNA-protein sequences.

    Main Results:

    • An SVM model using DNA data achieved 68.9% accuracy.
    • An SVM model using both DNA and protein sequences achieved 71.4% accuracy.
    • Prediction accuracy for double-stranded DNA binding sites was comparable to single-stranded molecules.

    Conclusions:

    • Protein binding site prediction in double-stranded DNA is feasible with comparable accuracy to single-stranded DNA.
    • Integrating both DNA and protein sequence data enhances prediction performance.
    • Developed SVM models and datasets are publicly available for research.