Related Experiment Video
Updated: Jan 27, 2026

06:24
Author Spotlight: Advancements in the Fabrication of Synthetic Vocal Fold Models for Phonetic and Robotic Applications
Published on: January 5, 2024
1.3K
Neurophysiological Muscle Activation Scheme for Controlling Vocal Fold Models
Summary
This study introduces a new model for vocal fold dynamics, incorporating natural neurological fluctuations in muscle activation. This approach better explains voice variability and pitch control, advancing our understanding of voice production.
Area of Science:
- Biomechanics of speech and voice production
- Computational modeling of the larynx
- Neurophysiology of vocalization
Background:
- Existing lumped-element vocal fold models often simplify muscle activation.
- Neurological fluctuations in laryngeal muscle activity are inherent to voice production.
- Understanding these fluctuations is crucial for explaining voice variability.
Purpose of the Study:
- To develop a physiologically-based scheme for vocal fold modeling that includes inherent neurological fluctuations.
- To investigate the impact of these stochastic muscle activation components on voice production dynamics.
- To assess the model's ability to replicate observed variability in vocal fold behavior.
Main Methods:
- Developed a lumped-element vocal fold model incorporating stochastic components in neural firing rate and motor unit recruitment.
- Utilized a body-cover model for vocal fold dynamics.
- Performed parametric analysis on steady-state sustained vowels to evaluate the effects of muscle activation fluctuations.
Main Results:
- Inherent muscle activation fluctuations introduce low and high-frequency components, varying with firing rate.
- The model demonstrated changes in system dynamics, including fundamental frequency fluctuations and unstable behavior near bifurcations.
- Stochastic components significantly impact vocal fold parameters, fine structure variability, and pitch control accuracy.
Conclusions:
- The proposed physiologically-based scheme provides a novel approach for controlling lumped-element voice production models.
- The model accurately reflects experimental observations of vocal fold variability and muscle activation signals.
- This framework can be extended to study voice production in neuropathological conditions.
Related Concept Videos
Protein Folding
127.2K
Overview
127.2K
Protein Folding
11.3K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.3K
The Z-Scheme of Electron Transport in Photosynthesis
13.4K
The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
13.4K
Molecular Chaperones and Protein Folding
19.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
19.7K
Molecular Chaperones and Protein Folding
14.9K
14.9K
Protein Folding Quality Check in the RER
5.1K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.1K

