Related Experiment Video

Updated: Aug 10, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Two distinct transpeptidation reactions during murein synthesis in Escherichia coli

W Kraus, J V Höltje

    Journal of Bacteriology
    |July 1, 1987
    PubMed

    More Related Videos

    Isolation and Preparation of Bacterial Cell Walls for Compositional Analysis by Ultra Performance Liquid Chromatography11:18

    Isolation and Preparation of Bacterial Cell Walls for Compositional Analysis by Ultra Performance Liquid Chromatography

    Published on: January 15, 2014

    Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking11:33

    Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

    Published on: December 17, 2013

    Related Concept Videos

    Mismatch Repair01:36

    Mismatch Repair

    Overview
    Insertion of Single-pass Transmembrane Proteins in the RER01:26

    Insertion of Single-pass Transmembrane Proteins in the RER

    Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
    Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
    Insertion of Multi-pass Transmembrane Proteins in the RER01:29

    Insertion of Multi-pass Transmembrane Proteins in the RER

    The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
    The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
    Protein Modifications in the RER01:26

    Protein Modifications in the RER

    Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
    Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
    Mismatch Repair01:20

    Mismatch Repair

    Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
    The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
    The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
    Peptidoglycan Synthesis01:28

    Peptidoglycan Synthesis

    Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...