Related Experiment Video

Updated: Aug 14, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

[Investigation of folding/unfolding kinetics of apomyoglobin]

E N Baryshnikova, B S Mel'nik, G V Semisotnov

    Molekuliarnaia Biologiia
    |December 20, 2005
    PubMed

    More Related Videos

    Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy10:09

    Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

    Published on: April 28, 2011

    OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy08:34

    OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

    Published on: February 5, 2020

    Related Concept Videos

    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...
    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...
    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...