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Related Concept Videos

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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Updated: May 7, 2026

A Structured Rehabilitation Protocol for Improved Multifunctional Prosthetic Control: A Case Study
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A Structured Rehabilitation Protocol for Improved Multifunctional Prosthetic Control: A Case Study

Published on: November 6, 2015

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A Customizable Fitting Protocol for the Body-Machine Interface.

Fiona A Neylon, Andrew Thompson, Rachel Kalvakota

    IEEE ... International Conference on Rehabilitation Robotics : [Proceedings]
    |July 11, 2025
    PubMed
    Summary
    This summary is machine-generated.

    A one-size-fits-all approach is insufficient for fitting a Body-Machine Interface (BoMI) for individuals with spinal cord injury. A flexible, clinically informed fitting protocol significantly improves robotic arm control and user experience.

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    Area of Science:

    • Biomedical Engineering
    • Rehabilitation Technology
    • Human-Computer Interaction

    Background:

    • Body-Machine Interfaces (BoMI) offer potential for individuals with motor impairments to control external devices.
    • Existing BoMI fitting methods may not adequately address severe upper extremity limitations in users with cervical spinal cord injury.

    Purpose of the Study:

    • To compare two methods of fitting a BoMI for robotic arm control in an individual with cervical spinal cord injury.
    • To develop and evaluate a novel, clinically informed customization and fitting protocol for BoMI systems.

    Main Methods:

    • Case study evaluation comparing a standardized BoMI fitting strategy with a flexible, clinically informed protocol.
    • Development of the BoMI Customization Evaluation (BCE) based on clinical assessment and user feedback.

    Main Results:

    • A one-size-fits-all BoMI placement strategy proved insufficient for users with severe upper extremity limitations.
    • The flexible fitting protocol led to improvements in BoMI map fitting success and robotic task performance.

    Conclusions:

    • A standardized fitting approach is inadequate for optimizing BoMI performance in users with significant motor impairments.
    • A novel, clinically integrated fitting protocol (BCE) shows promise for enhancing BoMI usability and effectiveness for individuals with spinal cord injury.