Related Experiment Video

Updated: Jun 27, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

Interview: Protein folding and studies of neurodegenerative diseases

Susan Lindquist

    Journal of Visualized Experiments : Jove
    |December 11, 2008
    PubMed

    More Related Videos

    Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans09:18

    Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

    Published on: September 7, 2021

    Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain09:00

    Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

    Published on: April 28, 2022

    Related Concept Videos

    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
    Protein Folding01:22

    Protein Folding

    Overview
    Protein Folding01:25

    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
    Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
    Protein Folding01:22

    Protein Folding

    Overview
    Molecular Chaperones and Protein Folding03:00

    Molecular Chaperones and Protein Folding

    The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
    The...