Related Experiment Video

Updated: Aug 18, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

[Spatial structure of myelopeptides: I. Conformational analysis of MP-1, MP-2, and MP-3]

N A Akhmetov, L I Ismailova, R M Abbasly

    Bioorganicheskaia Khimiia
    |March 25, 2005
    PubMed

    More Related Videos

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web09:51

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

    Published on: July 16, 2017

    Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities11:44

    Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

    Published on: October 2, 2018

    Related Concept Videos

    Microtubule Associated Proteins (MAPs)01:42

    Microtubule Associated Proteins (MAPs)

    Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
    Translocation of Proteins into the Mitochondria01:19

    Translocation of Proteins into the Mitochondria

    Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
    Sorting of outer membrane proteins:
    Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
    Protein Organization01:13

    Protein Organization

    Overview
    Assembly of Complex Microtubule Structures01:32

    Assembly of Complex Microtubule Structures

    Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
    Protein and Protein Structure02:15

    Protein and Protein Structure

    Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
    A protein's shape is critical to its function. For example, an enzyme can...
    Overview of Myosin Structure and Function01:15

    Overview of Myosin Structure and Function

    Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.