Related Experiment Video

Updated: Apr 15, 2026

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

17.9K

[Modification of [PSI+] prion properties by the combination of amino acid changes within Sup35 protein N-domain]

S A Bondarev, E D Shirokolobova, N P Trubitsyna

    Molekuliarnaia Biologiia
    |April 9, 2015
    PubMed

    More Related Videos

    Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis10:03

    Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

    Published on: July 16, 2008

    28.7K
    High-throughput Screening for Protein-based Inheritance in S. cerevisiae08:12

    High-throughput Screening for Protein-based Inheritance in S. cerevisiae

    Published on: August 8, 2017

    6.8K

    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,...
    13.1K
    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...
    12.7K
    Protein Folding01:22

    Protein Folding

    Overview
    131.3K
    Conservation of Protein Domains Over Different Proteins02:26

    Conservation of Protein Domains Over Different Proteins

    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...
    15.1K
    Bacterial Protein Maturation01:26

    Bacterial Protein Maturation

    Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
    730
    Conservation of Protein Domains02:26

    Conservation of Protein Domains

    4.4K