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Published on: January 16, 2016
Protein dynamics and the enzymatic reaction coordinate
1Department of Chemistry, University of Arizona, 1306 East University Blvd., Tucson, AZ, 85721, USA, steve.schwartz@einstein.yu.edu.
Topics in Current Chemistry
|March 20, 2013
Summary
Protein dynamics, including motions on ultrafast timescales, are crucial for enzyme function and chemical reactions. Advanced computational methods reveal how these protein movements directly influence the reaction coordinate.
Area of Science:
- Biochemistry
- Chemical Dynamics
- Structural Biology
Background:
- Enzyme catalysis involves complex chemical transformations.
- The role of protein dynamics in enzymatic reactions has been a subject of intense research.
- Understanding the interplay between protein motion and chemical reactions is key to enzyme function.
Purpose of the Study:
- To review the progress in understanding protein dynamics in enzyme catalysis over the last 15 years.
- To highlight the significance of protein motions across various timescales in enzymatic reactions.
- To discuss the direct coupling of ultrafast protein motions to chemical transformations.
Main Methods:
- Review of computational and experimental approaches in studying protein dynamics.
- Analysis of transition path sampling techniques.
- Application of committor analysis to understand reaction mechanisms.
Main Results:
- Protein motions from femtoseconds to milliseconds contribute to enzyme function.
- Sub-picosecond protein motions are directly coupled to chemical transformations in some enzymes.
- These ultrafast motions are integral to the reaction coordinate.
Conclusions:
- Protein dynamics are fundamental to enzymatic chemical reactions.
- Ultrafast protein motions play a direct role in facilitating chemical transformations.
- Advanced computational methods have significantly advanced the understanding of these dynamic processes.
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