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Journal article
Investigating the Effects of Molecular Crowding on the Kinetics of Protein Aggregation
The journal of physical chemistry. B, v 124(44), pp 9829-9839
05 Nov 2020
PMID: 33104345
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The thermodynamics and kinetics of protein folding and protein aggregation in vivo are of great importance in numerous scientific areas including fundamental biophysics research, nanotechnology, and medicine. However, these processes remain poorly understood in both in vivo and in vitro systems. Here we extend an established model for protein aggregation that is based on the kinetic equations for the moments of the polymer size distribution by introducing macromolecular crowding particles into the model using scaled-particle and transition-state theories. The model predicts that the presence of crowders can either speed up, cause no change to, or slow down the progress of the aggregation compared to crowder-free solutions, in striking agreement with experimental results from nine different amyloid-forming proteins that utilized dextran as the crowder. These different dynamic effects of macromolecular crowding can be understood in terms of the change of excluded volume associated with each reaction step.
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Details
- Title
- Investigating the Effects of Molecular Crowding on the Kinetics of Protein Aggregation
- Creators
- John S Schreck - Drexel UniversityJohn Bridstrup - Drexel UniversityJian-Min Yuan - Drexel University
- Publication Details
- The journal of physical chemistry. B, v 124(44), pp 9829-9839
- Publisher
- American Chemical Society; Washington, DC
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000589918200008
- Scopus ID
- 2-s2.0-85095749175
- Other Identifier
- 991019169036104721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Chemistry, Physical