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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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Molecular Chaperones and Protein Folding

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Related Experiment Video

Updated: May 24, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

HORIBALFRE program: Higher Order Residue Interactions Based ALgorithm for Fold REcognition.

Pandurangan Sundaramurthy, Raashi Sreenivasan, Khader Shameer

    Bioinformation
    |February 23, 2012
    PubMed
    Summary
    This summary is machine-generated.

    A new algorithm, HORIBALFRE, enhances protein fold recognition by analyzing higher-order residue interactions. Incorporating quadruplet interactions significantly improves the accuracy of identifying remote protein homology.

    Keywords:
    fold prediction algorithmfold recognitionhigher order residue interactionsprotein foldingresidue interactions

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    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

    Area of Science:

    • Structural bioinformatics
    • Computational biology
    • Protein structure prediction

    Background:

    • Protein function and structure prediction from novel genes is challenging.
    • Existing fold recognition methods struggle with remote homology detection.
    • Understanding protein structure is crucial for genomics and personalized medicine.

    Purpose of the Study:

    • To develop a novel algorithm, HORIBALFRE, for enhanced protein fold recognition.
    • To improve the detection of remote homology between protein sequences.
    • To leverage higher-order residue interactions for more accurate structure prediction.

    Main Methods:

    • Developed the Higher Order Residue Interaction Based ALgorithm for Fold REcognition (HORIBALFRE).
    • Incorporated pairwise, triplet, and quadruplet residue interactions into the algorithm.
    • Utilized a protein structure library from the CAMPASS database and Fischer's dataset (SCOP).
    • Performed sequence alignment using TCoffee for template and target sequences.

    Main Results:

    • HORIBALFRE successfully incorporates higher-order residue interactions.
    • The inclusion of quadruplet interactions demonstrably improves fold recognition accuracy.
    • Initial results indicate enhanced capability in detecting remote protein homology.

    Conclusions:

    • Higher-order residue interactions, particularly quadruplets, are vital for protein structure.
    • HORIBALFRE represents a promising advancement in potential-based fold recognition.
    • The algorithm offers improved accuracy for identifying evolutionary relationships between proteins.