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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
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A comprehensive database of verified experimental data on protein folding kinetics
Amy S Wagaman1, Aaron Coburn, Itai Brand-Thomas
1Department of Mathematics and Statistics, Amherst College, Amherst, Massachusetts.
Protein Science : a Publication of the Protein Society
|September 18, 2014
Summary
Researchers created ACPro, a curated protein folding database, by verifying experimental data. This resource aids computational model development and advances understanding of protein folding, stability, and dynamics.
Area of Science:
- Biophysics
- Computational Biology
- Structural Biology
Background:
- Protein folding is crucial for biological function, yet understanding its kinetics requires high-quality experimental data.
- Computational models for protein folding prediction need reliable datasets for validation.
Purpose of the Study:
- To create a comprehensive and verified database of protein folding rate constants.
- To facilitate the testing and development of computational protein folding models.
- To establish a standardized resource for the protein folding research community.
Main Methods:
- Compiled protein folding rate constants from 15 published collections and web databases.
- Verified each entry's folding rate (lnkf) and experimental conditions against original reports.
- Developed a streamlined submission form for new data adhering to established standards.
Main Results:
- Created ACPro, a curated database containing 126 verified protein folding kinetics entries.
- The database is freely accessible online, supporting the protein folding research community.
- Established a standardized method for incorporating new experimental folding kinetics data.
Conclusions:
- ACPro provides a high-confidence, accessible resource for validating protein folding models.
- The database promotes a stronger synergy between experimental and theoretical approaches in protein folding research.
- This resource will accelerate insights into protein folding, stability, and dynamics.
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