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Related Concept Videos

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 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 Organization01:13

Protein Organization

Overview
Protein Organization01:13

Protein Organization

Overview
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...

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Related Experiment Video

Updated: May 30, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

A rapid protein structure alignment algorithm based on a text modeling technique.

Jafar Razmara, Safaai Deris, Sepideh Parvizpour

    Bioinformation
    |August 5, 2011
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a novel protein structural alignment algorithm using text modeling. The method achieves competitive accuracy and high running speed, improving structural biology analysis.

    Keywords:
    protein structure alignmentsequence alignmenttext modeling

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    Last Updated: May 30, 2026

    A Protocol for Computer-Based Protein Structure and Function Prediction
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    Published on: November 3, 2011

    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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    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
    09:51

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

    Published on: July 16, 2017

    Area of Science:

    • Structural biology
    • Bioinformatics
    • Computational biology

    Background:

    • Protein structural alignment is crucial for understanding protein function and evolution.
    • Existing methods face challenges in accuracy and efficiency for large-scale analysis.

    Purpose of the Study:

    • To develop and evaluate a new algorithm for protein structural alignment.
    • To leverage text modeling techniques for enhanced alignment accuracy and speed.

    Main Methods:

    • Superimposing secondary structure elements of proteins.
    • Modeling 3D protein structures as sequences of alphabets.
    • Employing a step-by-step sequence alignment procedure for structural comparison.

    Main Results:

    • The algorithm demonstrates competitive accuracy compared to state-of-the-art methods like CE and TM-align.
    • The method achieves high running speeds, comparable to 3D-BLAST.
    • Benchmark tests on 200 non-homologous proteins validate the program's performance.

    Conclusions:

    • The text modeling-based algorithm offers a promising approach for accurate and efficient protein structural alignment.
    • This method can significantly benefit structural biology research and applications.