Related Experiment Video

Updated: May 23, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

[Classification of self-organizing peptides]

A V Danilkovich, V M Lipkin, I P Udovichenko

    Bioorganicheskaia Khimiia
    |April 14, 2012
    PubMed

    More Related Videos

    A Tripeptide-Stabilized Nanoemulsion of Oleic Acid10:42

    A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

    Published on: February 27, 2019

    Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self-Assembling Peptide Matrix10:23

    Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self-Assembling Peptide Matrix

    Published on: May 3, 2024

    Related Concept Videos

    Signal Sequences and Sorting Receptors01:41

    Signal Sequences and Sorting Receptors

    Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
    Peptide Identification Using Tandem Mass Spectrometry01:33

    Peptide Identification Using Tandem Mass Spectrometry

    Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
    This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
    Protein Organization01:24

    Protein Organization

    Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
    The primary structure of a protein is its amino acid sequence.
    Protein Organization01:13

    Protein Organization

    Overview
    Protein Complex Assembly02:41

    Protein Complex Assembly

    Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
    Many viruses self-assemble into a fully functional unit using the infected host cell to...
    Peptide Bonds02:43

    Peptide Bonds

    A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...