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Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies
Chitra Narayanan1, David N Bernard1, Nicolas Doucet2
1INRS-Institut Armand-Frappier, Université du Québec, 531 Boul. des Prairies, Laval, QC H7V 1B7, Canada (C.N.).
Catalysts (Basel, Switzerland)
|April 4, 2017
Summary
Enzymes use complex atomic movements for function, but their exact role is unclear. This review explains methods to study these dynamics and apply findings to enzyme systems like HIV-1 protease.
Area of Science:
- Biochemistry
- Structural Biology
- Computational Biology
Background:
- Enzymes are dynamic entities crucial for biological processes.
- The precise role of enzyme dynamics in function is not fully understood.
- Understanding protein motion is key to interpreting enzyme mechanisms.
Purpose of the Study:
- To bridge the gap between biophysical observations and biological significance of enzyme dynamics.
- To review methodologies for characterizing atomic-scale motions in enzymes.
- To illustrate the application of dynamics knowledge in understanding and manipulating enzyme function.
Main Methods:
- Experimental techniques to probe residue motions across various timescales.
- Computational methodologies for analyzing enzyme dynamics.
- Case studies on HIV-1 protease and DNA polymerase β.
Main Results:
- Common experimental and computational methods for studying enzyme dynamics are described.
- Knowledge of atomic-scale motions can elucidate enzyme function.
- Dynamics information can potentially be used to modulate enzyme activity.
Conclusions:
- Enzyme dynamics are integral to ligand recognition and catalysis.
- Characterizing protein motions provides insights into enzyme mechanisms.
- Studying dynamics offers avenues for enzyme engineering and drug design.