Related Experiment Video

Updated: Jul 21, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Localization of a new proteolytic site accessible in oxidized myosin rod

L Nyitray, G Mócz, M Bálint

    FEBS Letters
    |February 25, 1985
    PubMed

    More Related Videos

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays08:57

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

    Published on: February 4, 2021

    Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability12:26

    Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

    Published on: June 2, 2023

    Related Concept Videos

    Conserved Binding Sites01:49

    Conserved Binding Sites

    Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
    Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
    Ligand Binding and Linkage00:49

    Ligand Binding and Linkage

    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
    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.
    Actin and Myosin in Muscle Contraction01:16

    Actin and Myosin in Muscle Contraction

    Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
    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,...
    Allosteric Proteins-ATCase01:19

    Allosteric Proteins-ATCase

    Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
    Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...