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Related Concept Videos

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.
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,...
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Genome Annotation and Assembly03:36

Genome Annotation and Assembly

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The genome refers to all of the genetic material in an organism. It can range from a few million base pairs in microbial cells to several billion base pairs in many eukaryotic organisms. Genome assembly refers to the process of taking the DNA sequencing data and putting it all back together in a correct order to create a close representation of the original genome. This is followed by the identification of functional elements on the newly assembled genome, a process called genome annotation.
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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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Swin-PSAxialNet: An Efficient Multi-Organ Segmentation Technique
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A Sub-Sequence Based Approach to Protein Function Prediction via Multi-Attention Based Multi-Aspect Network.

Ashish Ranjan, Archana Tiwari, Akshay Deepak

    IEEE/ACM Transactions on Computational Biology and Bioinformatics
    |November 26, 2021
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a novel multi-aspect method for protein sub-sequence classification, improving protein function prediction. The Global-ProtEnc-Plus model achieved outstanding performance on the CAFA3 dataset.

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    A Protocol for Computer-Based Protein Structure and Function Prediction
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    A Protocol for Computer-Based Protein Structure and Function Prediction

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    Area of Science:

    • Bioinformatics
    • Computational Biology
    • Protein Science

    Background:

    • Protein function prediction is crucial for understanding biological processes.
    • Classifying protein sub-sequences is challenging due to limited knowledge of sub-sequence functions.
    • Existing methods often struggle to efficiently utilize parent sequence information for sub-sequence classification.

    Purpose of the Study:

    • To develop a novel "multi-aspect" paradigm for efficient protein sub-sequence classification.
    • To propose the "Multi-Attention Based Multi-Aspect Network" for sub-sequence classification.
    • To introduce the Global-ProtEnc method for protein sequence encoding and function prediction.

    Main Methods:

    • Developed a "multi-aspect" paradigm incorporating multi-label and label-relevance scoring.
    • Proposed the "Multi-Attention Based Multi-Aspect Network" utilizing word-level multi-attention for sub-sequence processing.
    • Introduced Global-ProtEnc, a sub-sequence-based encoding approach, and its ensemble version, Global-ProtEnc-Plus.

    Main Results:

    • Global-ProtEnc and Global-ProtEnc-Plus demonstrated outstanding performance on the CAFA3 benchmark dataset.
    • Global-ProtEnc-Plus showed significant improvements over the state-of-the-art DeepGOPlus.
    • Specific improvements include +6.50% Fmax for biological process and +1.90% for cellular component prediction.

    Conclusions:

    • The proposed multi-aspect paradigm and Global-ProtEnc methods enhance protein sub-sequence classification and function prediction.
    • Global-ProtEnc-Plus represents a significant advancement in protein function prediction accuracy.
    • These methods offer efficient and effective tools for analyzing protein sequences and their functions.