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Related Concept Videos

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
The Sarcomere01:08

The Sarcomere

A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each myosin...
Introduction to Actin01:26

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across different species.
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...

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Related Experiment Video

Updated: Jun 11, 2026

The Mechanics of (Poro-)Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
08:50

The Mechanics of (Poro-)Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton

Published on: March 10, 2023

The actin-myosin interface.

Michael Lorenz1, Kenneth C Holmes

  • 1Biophysics Group, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Michael.Lorenz@mpimf-heidelberg.mpg.de

Proceedings of the National Academy of Sciences of the United States of America
|July 10, 2010
PubMed
Summary
This summary is machine-generated.

Understanding muscle contraction requires knowing how myosin binds actin. This study used a novel technique to create an atomic model of the actin-myosin interface, revealing extensive contacts crucial for muscle function.

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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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The Mechanics of (Poro-)Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Muscle contraction is a fundamental biological process.
  • Understanding the atomic-level interactions between actin and myosin is key to elucidating muscle function.
  • The reversible binding of myosin to actin is essential for muscle contraction.

Purpose of the Study:

  • To obtain an atomic model of the strong-binding (rigor) actin-myosin interface.
  • To investigate the mechanism of myosin binding to actin at the atomic level.
  • To understand the structural basis of actin-myosin interactions in muscle.

Main Methods:

  • Utilized a novel molecular dynamics technique.
  • Constrained simulations using an electron microscopy (EM) map of the actin-myosin complex at 13-Å resolution.
  • Developed an atomic model of the actin-myosin interface.

Main Results:

  • The molecular dynamics simulation successfully converted myosin from a weak-binding to a strong-binding (rigor) state.
  • The resulting atomic model reveals extensive contacts between actin and the myosin head (S1), spanning two actin monomers.
  • The contact surface area is significantly larger than in previous models, involving multiple loops from both actin and S1.

Conclusions:

  • The study provides a high-resolution atomic model of the strong-binding actin-myosin interface.
  • The findings suggest a detailed structural mechanism for actin-myosin interaction during muscle contraction.
  • The model offers insights into the potential role of specific mutations, such as Arg 405 Glu in S1, in familial cardiomyopathy.