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Related Concept Videos

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.
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
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...
Excitation-Contraction Coupling in Skeletal Muscles01:20

Excitation-Contraction Coupling in Skeletal Muscles

Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
When an action potential...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...

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Related Experiment Video

Updated: May 14, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
06:53

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Structural insight into the UNC-45-myosin complex.

Filip Fratev1, Svava Osk Jónsdóttir, Ilza Pajeva

  • 1Micar 21 Ltd., 1470 Sofia, Bulgaria. fratev@clbme.bas.bg

Proteins
|February 15, 2013
PubMed
Summary
This summary is machine-generated.

The UNC-45 chaperone protein

More Related Videos

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
09:38

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Published on: July 1, 2021

Related Experiment Videos

Last Updated: May 14, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
06:53

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
09:38

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Published on: July 1, 2021

Area of Science:

  • Structural biology
  • Biochemistry
  • Computational modeling

Background:

  • UNC-45 chaperone protein is crucial for myosin function, stability, and ATPase activity.
  • It plays a significant role in cardiomyopathy and breast cancer progression.

Purpose of the Study:

  • To develop the first in silico structural model of the UNC-45-myosin complex.
  • To elucidate the structural basis of UNC-45's interaction with cardiac myosin (MYH7).

Main Methods:

  • Identification of the human UNC-45B binding epitope.
  • Molecular docking of UNC-45B to the MYH7 motor domain.
  • Extensive molecular dynamics simulations (630 ns) to refine the complex structure.

Main Results:

  • A stable UNC45B-MYH7 complex model was generated, primarily stabilized by electrostatic interactions.
  • The contact surface area is comparable to the myosin-actin complex interface.
  • Significant interspecies variations in the myosin binding epitope were identified.

Conclusions:

  • The study provides a detailed structural model of the UNC-45B-MYH7 complex.
  • Reveals the structural underpinnings of MYH7 mutations linked to hypertrophic cardiomyopathy.
  • Offers insights for developing targeted therapeutic strategies for myosin-related diseases.