Motor Protein Dynamics

Motor protein dynamics describes how molecular motors generate force and movement by interacting with cytoskeletal filaments, making them central to intracellular transport, cell organization, and mechanobiology. Powered by ATP hydrolysis, proteins such as kinesin, dynein, and myosin undergo conformational changes that produce directed stepping, cargo movement, or filament sliding under load. In bioengineering, studying these dynamics helps researchers quantify nanoscale force production, design biomolecular transport systems, and develop synthetic materials that mimic cellular motion. Experimental and computational analyses of stepping rates, processivity, and load dependence also support advances in drug delivery, biosensors, tissue engineering, and molecular robotics.

Motor Protein Dynamics - Related Videos

Education

JoVE Core - Cell Biology

Microtubule Associated Motor Proteins

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2023

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...

Research

JoVE EoE - Neuropathology

Immunoprecipitation of Target Protein-DNA Complexes from Motor Neuron Lysate

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2025

This video demonstrates the immunoprecipitation of DNA fragments crosslinked with target protein from stem cell-derived motor neuron lysates using target protein-specific antibody-coated magnetic beads.

Research

JoVE Journal - Biochemistry
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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Cited by 2 •

2017

A protocol for the online investigation of protein sequence-structure-dynamics relationships using Bio3D-web is presented.

Research

JoVE Journal - Bioengineering
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Dynamic Light-Induced Protein Patterns at Model Membranes

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Cited by 2 •

2024

Here, a protocol is described for generating light-regulated and reversible protein patterns with high spatiotemporal precision at artificial lipid membranes. The method consists of the localized photoactivation of the protein iLID (improved light-inducible dimer) immobilized on model membranes that, under blue light, binds to its partner protein Nano (wild-type SspB).

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

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Cited by 4 •

2025

Plasmonic nanotweezers use localized surface plasmon resonance in gold nanostructures to trap single nanoparticles, including proteins, within a nanometer-scale optical field. Changes in the scattered signal reveal protein presence and conformational dynamics, enabling monitoring without fluorophore modifications or surface tethering.

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